A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity.
The subfamily of myosin proteins that are commonly found in muscle fibers. Myosin II is also involved a diverse array of cellular functions including cell division, transport within the GOLGI APPARATUS, and maintaining MICROVILLI structure.
Parts of the myosin molecule resulting from cleavage by proteolytic enzymes (PAPAIN; TRYPSIN; or CHYMOTRYPSIN) at well-localized regions. Study of these isolated fragments helps to delineate the functional roles of different parts of myosin. Two of the most common subfragments are myosin S-1 and myosin S-2. S-1 contains the heads of the heavy chains plus the light chains and S-2 contains part of the double-stranded, alpha-helical, heavy chain tail (myosin rod).
The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins.
A subclass of myosin involved in organelle transport and membrane targeting. It is abundantly found in nervous tissue and neurosecretory cells. The heavy chains of myosin V contain unusually long neck domains that are believed to aid in translocating molecules over large distances.
A nonmuscle isoform of myosin type II found predominantly in platelets, lymphocytes, neutrophils and brush border enterocytes.
A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.
A nonmuscle isoform of myosin type II found predominantly in neuronal tissue.
Myosin type II isoforms found in cardiac muscle.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
An enzyme that phosphorylates myosin light chains in the presence of ATP to yield myosin-light chain phosphate and ADP, and requires calcium and CALMODULIN. The 20-kDa light chain is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors. The enzyme plays a central role in the regulation of smooth muscle contraction.
A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.
Myosin type II isoforms found in smooth muscle.
A subclass of myosins originally found in the photoreceptor of DROSOPHILA. The heavy chains can occur as two alternatively spliced isoforms of 132 and 174 KDa. The amino terminal of myosin type III is highly unusual in that it contains a protein kinase domain which may be an important component of the visual process.
Myosin type II isoforms found in skeletal muscle.
Contractile tissue that produces movement in animals.
A class of organic compounds containing four or more ring structures, one of which is made up of more than one kind of atom, usually carbon plus another atom. The heterocycle may be either aromatic or nonaromatic.
A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.
Isoforms of MYOSIN TYPE II, specifically found in the ventricular muscle of the HEART. Defects in the genes encoding ventricular myosins result in FAMILIAL HYPERTROPHIC CARDIOMYOPATHY.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Proteins that are involved in or cause CELL MOVEMENT such as the rotary structures (flagellar motor) or the structures whose movement is directed along cytoskeletal filaments (MYOSIN; KINESIN; and DYNEIN motor families).
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.
Unstriated and unstriped muscle, one of the muscles of the internal organs, blood vessels, hair follicles, etc. Contractile elements are elongated, usually spindle-shaped cells with centrally located nuclei. Smooth muscle fibers are bound together into sheets or bundles by reticular fibers and frequently elastic nets are also abundant. (From Stedman, 25th ed)
A genus of protozoa, formerly also considered a fungus. Its natural habitat is decaying forest leaves, where it feeds on bacteria. D. discoideum is the best-known species and is widely used in biomedical research.
A process leading to shortening and/or development of tension in muscle tissue. Muscle contraction occurs by a sliding filament mechanism whereby actin filaments slide inward among the myosin filaments.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
The long cylindrical contractile organelles of STRIATED MUSCLE cells composed of ACTIN FILAMENTS; MYOSIN filaments; and other proteins organized in arrays of repeating units called SARCOMERES .
Large woodland game BIRDS in the subfamily Meleagridinae, family Phasianidae, order GALLIFORMES. Formerly they were considered a distinct family, Melegrididae.
A protein found in the thin filaments of muscle fibers. It inhibits contraction of the muscle unless its position is modified by TROPONIN.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.
The rate dynamics in chemical or physical systems.
A group of intracellular-signaling serine threonine kinases that bind to RHO GTP-BINDING PROTEINS. They were originally found to mediate the effects of rhoA GTP-BINDING PROTEIN on the formation of STRESS FIBERS and FOCAL ADHESIONS. Rho-associated kinases have specificity for a variety of substrates including MYOSIN-LIGHT-CHAIN PHOSPHATASE and LIM KINASES.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
Large, multinucleate single cells, either cylindrical or prismatic in shape, that form the basic unit of SKELETAL MUSCLE. They consist of MYOFIBRILS enclosed within and attached to the SARCOLEMMA. They are derived from the fusion of skeletal myoblasts (MYOBLASTS, SKELETAL) into a syncytium, followed by differentiation.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
A phylum of the kingdom Metazoa. Mollusca have soft, unsegmented bodies with an anterior head, a dorsal visceral mass, and a ventral foot. Most are encased in a protective calcareous shell. It includes the classes GASTROPODA; BIVALVIA; CEPHALOPODA; Aplacophora; Scaphopoda; Polyplacophora; and Monoplacophora.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
A genus of ameboid protozoa. Characteristics include a vesicular nucleus and the formation of several lodopodia, one of which is dominant at a given time. Reproduction occurs asexually by binary fission.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
The repeating contractile units of the MYOFIBRIL, delimited by Z bands along its length.
Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
A genus of free-living soil amoebae that produces no flagellate stage. Its organisms are pathogens for several infections in humans and have been found in the eye, bone, brain, and respiratory tract.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
A subclass of myosin found in ACANTHAMOEBA. It is a non-filamentous myosin containing a single 180-kDa myosin heavy chain.
Myosin type II isoforms specifically found in the atrial muscle of the heart.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The movement of CYTOPLASM within a CELL. It serves as an internal transport system for moving essential substances throughout the cell, and in single-celled organisms, such as the AMOEBA, it is responsible for the movement (CELL MOVEMENT) of the entire cell.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Skeletal muscle fibers characterized by their expression of the Type I MYOSIN HEAVY CHAIN isoforms which have low ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment.
Developmental events leading to the formation of adult muscular system, which includes differentiation of the various types of muscle cell precursors, migration of myoblasts, activation of myogenesis and development of muscle anchorage.
Seven membered heterocyclic rings containing a NITROGEN atom.
Skeletal muscle fibers characterized by their expression of the Type II MYOSIN HEAVY CHAIN isoforms which have high ATPase activity and effect several other functional properties - shortening velocity, power output, rate of tension redevelopment. Several fast types have been identified.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The sum of the weight of all the atoms in a molecule.
Muscular contractions characterized by increase in tension without change in length.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
A large family of mollusks in the class BIVALVIA, known commonly as scallops. They possess flat, almost circular shells and are found in all seas from shallow water to great depths.
A giant elastic protein of molecular mass ranging from 2,993 kDa (cardiac), 3,300 kDa (psoas), to 3,700 kDa (soleus) having a kinase domain. The amino- terminal is involved in a Z line binding, and the carboxy-terminal region is bound to the myosin filament with an overlap between the counter-connectin filaments at the M line.
One of the minor protein components of skeletal muscle. Its function is to serve as the calcium-binding component in the troponin-tropomyosin B-actin-myosin complex by conferring calcium sensitivity to the cross-linked actin and myosin filaments.
Very toxic polypeptide isolated mainly from AMANITA phalloides (Agaricaceae) or death cup; causes fatal liver, kidney and CNS damage in mushroom poisoning; used in the study of liver damage.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
A powerful flexor of the thigh at the hip joint (psoas major) and a weak flexor of the trunk and lumbar spinal column (psoas minor). Psoas is derived from the Greek "psoa", the plural meaning "muscles of the loin". It is a common site of infection manifesting as abscess (PSOAS ABSCESS). The psoas muscles and their fibers are also used frequently in experiments in muscle physiology.
A white crystal or crystalline powder used in BUFFERS; FERTILIZERS; and EXPLOSIVES. It can be used to replenish ELECTROLYTES and restore WATER-ELECTROLYTE BALANCE in treating HYPOKALEMIA.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
Carrier of aroma of butter, vinegar, coffee, and other foods.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The process by which the CYTOPLASM of a cell is divided.

Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast. (1/5414)

Cell division in a number of eukaryotes, including the fission yeast Schizosaccharomyces pombe, is achieved through a medially placed actomyosin-based contractile ring. Although several components of the actomyosin ring have been identified, the mechanisms regulating ring assembly are still not understood. Here, we show by biochemical and mutational studies that the S.pombe actomyosin ring component Cdc4p is a light chain associated with Myo2p, a myosin II heavy chain. Localization of Myo2p to the medial ring depended on Cdc4p function, whereas localization of Cdc4p at the division site was independent of Myo2p. Interestingly, the actin-binding and motor domains of Myo2p are not required for its accumulation at the division site although the motor activity of Myo2p is essential for assembly of a normal actomyosin ring. The initial assembly of Myo2p and Cdc4p at the division site requires a functional F-actin cytoskeleton. Once established, however, F-actin is not required for the maintenance of Cdc4p and Myo2p medial rings, suggesting that the attachment of Cdc4p and Myo2p to the division site involves proteins other than actin itself.  (+info)

Regulation of chamber-specific gene expression in the developing heart by Irx4. (2/5414)

The vertebrate heart consists of two types of chambers, the atria and the ventricles, which differ in their contractile and electrophysiological properties. Little is known of the molecular mechanisms by which these chambers are specified during embryogenesis. Here a chicken iroquois-related homeobox gene, Irx4, was identified that has a ventricle-restricted expression pattern at all stages of heart development. Irx4 protein was shown to regulate the chamber-specific expression of myosin isoforms by activating the expression of the ventricle myosin heavy chain-1 (VMHC1) and suppressing the expression of the atrial myosin heavy chain-1 (AMHC1) in the ventricles. Thus, Irx4 may play a critical role in establishing chamber-specific gene expression in the developing heart.  (+info)

Association of a myosin immunoanalogue with cell envelopes of Aspergillus fumigatus conidia and its participation in swelling and germination. (3/5414)

A myosin immunoanalogue was identified in conidia of Aspergillus fumigatus by Western blotting, indirect immunofluorescence assay, and gold immunoelectron microscopy with two different antimyosin antibodies. The distribution pattern of this protein was followed during the early stages of germination. A single 180-kDa polypeptide, detected predominantly in a cell envelope extract, was found to cross-react with monoclonal and polyclonal antibodies raised against vertebrate muscle myosin. Immunoelectron microscopy permitted precise localization of this polypeptide, indicating that myosin analogue was mainly distributed along the plasma membrane of resting and swollen conidia. In germinating conidia, indirect immunofluorescence microscopy revealed myosin analogue at the periphery of germ tubes, whereas actin appeared as dispersed punctate structures in the cytoplasm that were more concentrated at the site of germ tube emergence. A myosin ATPase inhibitor, butanedione monoxime, greatly reduced swelling and blocked germination. In contrast, when conidia were treated with cytochalasin B, an inhibitor of actin polymerization, swelling was not affected and germination was only partially reduced. Butanedione monoxime-treated conidia showed accumulation of cytoplasmic vesicles and did not achieve cell wall reorganization, unlike swollen conidia. Collectively, these results suggest an essential role for this myosin analogue in the deposition of cell wall components during germination of A. fumigatus conidia and therefore in host tissue colonization.  (+info)

Studies on a nonpolysomal ribonucleoprotein coding for myosin heavy chains from chick embryonic muscles. (4/5414)

A messenger ribonucleoprotein (mRNP) particle containing the mRNA coding for the myosin heavy chain (MHC mRNA) has been isolated from the postpolysomal fraction of homogenates of 14-day-old chick embryonic muscles. The mRNP sediments in sucrose gradient as 120 S and has a characteristic buoyant density of 1.415 g/cm3, which corresponds to an RNA:protein ratio of 1:3.8. The RNA isolated from the 120 S particle behaved like authentic MHC mRNA purified from chick embryonic muscles with respect to electrophoretic mobility and ability to program the synthesis of myosin heavy chain in a rabbit reticulocyte lysate system as judged by multi-step co-purification of the in vitro products with chick embryonic leg muscle myosin added as carrier. The RNA obtained from the 120 S particle was as effective as purified MHC mRNA in stimulating the synthesis of the complete myosin heavy chains in rabbit reticulocyte lysate under conditions where non-muscle mRNAs had no such effect. Analysis of the protein moieties of the 120 S particle by sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows the presence of seven distinct polypeptides with apparent molecular weights of 44,000, 49,000, 53,000, 81,000, 83,000, and 98,000, whereas typical ribosomal proteins are absent. These results indicate that the 120 S particles are distinct cellular entities unrelated to ribosomes or initiation complexes. The presence of muscle-specific mRNAs as cytoplasmic mRNPs suggests that these particles may be involved in translational control during myogenesis in embryonic muscles.  (+info)

Myosin II-independent F-actin flow contributes to cell locomotion in dictyostelium. (5/5414)

While the treadmilling and retrograde flow of F-actin are believed to be responsible for the protrusion of leading edges, little is known about the mechanism that brings the posterior cell body forward. To elucidate the mechanism for global cell locomotion, we examined the organizational changes of filamentous (F-) actin in live Dictyostelium discoideum. We labeled F-actin with a trace amount of fluorescent phalloidin and analyzed its dynamics in nearly two-dimensional cells by using a sensitive, high-resolution charge-coupled device. We optically resolved a cyclic mode of tightening and loosening of fibrous cortical F-actin and quantitated its flow by measuring temporal and spatial intensity changes. The rate of F-actin flow was evaluated with respect to migration velocity and morphometric changes. In migrating monopodial cells, the cortical F-actin encircling the posterior cell body gradually accumulated into the tail end at a speed of 0.35 microm/minute. We show qualitatively and quantitatively that the F-actin flow is closely associated with cell migration. Similarly, in dividing cells, the cortical F-actin accumulated into the cleavage furrow. Although five times slower than the wild type, the F-actin also flows rearward in migrating mhcA- cells demonstrating that myosin II ('conventional' myosin) is not absolutely required for the observed dynamics of F-actin. Yet consistent with the reported transportation of ConA-beads, the direction of observed F-actin flow in Dictyostelium is conceptually opposite from a barbed-end binding to the plasma membrane. This study suggests that the posterior end of the cell has a unique motif that tugs the cortical actin layer rearward by means of a mechanism independent from myosin II; this mechanism may be also involved in cleavage furrow formation.  (+info)

(CTG)n repeats markedly inhibit differentiation of the C2C12 myoblast cell line: implications for congenital myotonic dystrophy. (6/5414)

Although the mutation for myotonic dystrophy has been identified as a (CTG)n repeat expansion located in the 3'-untranslated region of a gene located on chromosome 19, the mechanism of disease pathogenesis is not understood. The objective of this study was to assess the effect of (CTG)n repeats on the differentiation of myoblasts in cell culture. We report here that C2C12 myoblast cell lines permanently transfected with plasmid expressing 500 bases long CTG repeat sequences, exhibited a drastic reduction in their ability to fuse and differentiate into myotubes. The percentage of cells fused into myotubes in C2 C12 cells (53.4+/-4.4%) was strikingly different from those in the two CTG repeat carrying clones (1.8+/-0.4% and 3.3+/-0. 7%). Control C2C12 cells permanently transfected with vector alone did not show such an effect. This finding may have important implications in understanding the pathogenesis of congenital myotonic dystrophy.  (+info)

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation. (7/5414)

It has been demonstrated previously that during mitosis the sites of myosin phosphorylation are switched between the inhibitory sites, Ser 1/2, and the activation sites, Ser 19/Thr 18 (Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. J. Cell Biol. 124:129- 137; Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. J. Cell Biol. 118:595-605), suggesting a regulatory role of myosin phosphorylation in cell division. To explore the function of myosin phosphatase in cell division, the possibility that myosin phosphatase activity may be altered during cell division was examined. We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mitosis-specific phosphorylation and that the phosphorylation is reversed during cytokinesis. MYPT phosphorylated either in vivo or in vitro in the mitosis-specific way showed higher binding to myosin II (two- to threefold) compared to MYPT from cells in interphase. Furthermore, the activity of myosin phosphatase was increased more than twice and it is suggested this reflected the increased affinity of myosin binding. These results indicate the presence of a unique positive regulatory mechanism for myosin phosphatase in cell division. The activation of myosin phosphatase during mitosis would enhance dephosphorylation of the myosin regulatory light chain, thereby leading to the disassembly of stress fibers during prophase. The mitosis-specific effect of phosphorylation is lost on exit from mitosis, and the resultant increase in myosin phosphorylation may act as a signal to activate cytokinesis.  (+info)

Calculation of a Gap restoration in the membrane skeleton of the red blood cell: possible role for myosin II in local repair. (8/5414)

Human red blood cells contain all of the elements involved in the formation of nonmuscle actomyosin II complexes (V. M. Fowler. 1986. J. Cell. Biochem. 31:1-9; 1996. Curr. Opin. Cell Biol. 8:86-96). No clear function has yet been attributed to these complexes. Using a mathematical model for the structure of the red blood cell spectrin skeleton (M. J. Saxton. 1992. J. Theor. Biol. 155:517-536), we have explored a possible role for myosin II bipolar minifilaments in the restoration of the membrane skeleton, which may be locally damaged by major mechanical or chemical stress. We propose that the establishment of stable links between distant antiparallel actin protofilaments after a local myosin II activation may initiate the repair of the disrupted area. We show that it is possible to define conditions in which the calculated number of myosin II minifilaments bound to actin protofilaments is consistent with the estimated number of myosin II minifilaments present in the red blood cells. A clear restoration effect can be observed when more than 50% of the spectrin polymers of a defined area are disrupted. It corresponds to a significant increase in the spectrin density in the protein free region of the membrane. This may be involved in a more complex repair process of the red blood cell membrane, which includes the vesiculation of the bilayer and the compaction of the disassembled spectrin network.  (+info)

We report the identification and characterization of myr 4 (myosin from rat), the first mammalian myosin I that is not closely related to brush border myosin I. Myr 4 contains a myosin head (motor) domain, a regulatory domain with light chain binding sites and a tail domain. Sequence analysis of myosin I head (motor) domains suggested that myr 4 defines a novel subclass of myosin Is. This subclass is clearly different from the vertebrate brush border myosin I subclass (which includes myr 1) and the myosin I subclass(es) identified from Acanthamoeba castellanii and Dictyostelium discoideum. In accordance with this notion, a detailed sequence analysis of all myosin I tail domains revealed that the myr 4 tail is unique, except for a newly identified myosin I tail homology motif detected in all myosin I tail sequences. The Ca(2+)-binding protein calmodulin was demonstrated to be associated with myr 4. Calmodulin binding activity of myr 4 was mapped by gel overlay assays to the two consecutive light ...
Myosins are actin-based motor proteins involved in many cellular movements. It is interesting to study the evolutionary patterns and the functional attributes of various types of myosins. Computational search algorithms were performed to identify putative myosin members by phylogenetic analysis, sequence motifs, and coexisting domains. This study is aimed at understanding the distribution and the likely biological functions of myosins encoded in various taxa and available eukaryotic genomes. We report here a phylogenetic analysis of around 4,064 myosin motor domains, built entirely from complete or near-complete myosin repertoires incorporating many unclassified, uncharacterized sequences and new myosin classes, with emphasis on myosins from Fungi, Haptophyta, and other Stramenopiles, Alveolates, and Rhizaria (SAR). The identification of large classes of myosins in Oomycetes, Cellular slime molds, Choanoflagellates, Pelagophytes, Eustigmatophyceae, Fonticula, Eucoccidiorida, and Apicomplexans ...
Conventional myosin (myosin II) is a major component of the cytoskeleton in a wide variety of eukaryotic cells, ranging from lower amoebae to mammalian fibroblasts and neutrophils. Gene targeting technologies available in the Dictyostelium discoideum system have provided the first genetic proof that this molecular motor protein is essential for normal cytokinesis, capping of cell surface receptors, normal chemotactic cell locomotion and morphogenetic shape changes during development. Although the roles of myosin in a variety of cell functions are becoming clear, the mechanisms that regulate myosin assembly into functional bipolar filaments within cells are poorly understood. Dictyostelium is currently the only system where mutant forms of myosin can be engineered in vitro, then expressed in their native context in cells that are devoid of the wild-type isoform. We have utilized this technology in combination with nested truncation and deletion analysis to map domains of the myosin tail ...
Using optical trapping and fluorescence imaging techniques, we measured the step size and stiffness of single skeletal myosins interacting with actin filaments and arranged on myosin-rod cofilaments that approximate myosin mechanics during muscle contraction. Stiffness is dramatically lower for negatively compared to positively strained myosins, consistent with buckling of myosins subfragment 2 rod domain. Low stiffness minimizes drag of negatively strained myosins during contraction at loaded conditions. Myosins elastic portion is stretched during active force generation, reducing apparent step size with increasing load, even though the working stroke is approximately constant at about 8 nanometers. Taking account of the nonlinear nature of myosin elasticity is essential to relate myosins internal structural changes to physiological force generation and filament sliding.. ...
TY - JOUR. T1 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW column. AU - Lema, Mark J.. AU - Pluskal, Malcolm G.. AU - Allen, Paul D.. PY - 1989. Y1 - 1989. N2 - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and smooth muscle. This method produces high-speed resolution (30-min analysis) of myosin from contaminating myofibrillar proteins. The column has a high capacity for binding myosin (up to 1 g) and can be used for small-scale preparation of highly purified myosin. Gel analysis in the presence of sodium dodecyl sulfate showed recovery of myosin with very little contamination of other myofibrillar proteins. Myosin was also recovered from small biopsy samples (0.1 g) by a direct extraction technique with recovery of biological ATPase activity.. AB - High-performance ion-exchange chromatography of myosin using a DEAE-5PW packing was used to purify myosin from skeletal, cardiac and ...
The docking of the heads onto the thick filament backbone may be directly relevant to the physiology of how muscles most efficiently maintain the relaxed state (2, 3). Several published three-dimensional (3D) reconstructions of relaxed myosin thick filaments (4-8) indicate that the heads are docked in an asymmetric structure known as the interacting heads motif (IHM) (Fig. 1D). The IHM was first observed in smooth muscle myosin and explained how smooth muscle myosin is switched on and off by phosphorylation (9). In the IHM, one head is called blocked because its actin-binding domain contacts the adjacent head and is therefore unavailable to bind actin. The other head is called free because its actin-binding domain is not obstructed and could theoretically bind actin. The IHM was originally thought to be specific to smooth and nonmuscle myosin but was later observed in thick filaments from tarantula (4, 10), scallop (8), Limulus (5), and human cardiac muscle (6, 7), leading to the suggestions ...
Muscle, motor unit and muscle fibre type-specific differences in force-generating capacity have been investigated for many years, but there is still no consensus regarding specific differences between slow- and fast-twitch muscles, motor units or muscle fibres. This is probably related to a number of different confounding factors disguising the function of the molecular motor protein myosin. We have therefore studied the force-generating capacity of specific myosin isoforms or combination of isoforms extracted from short single human muscle fibre segments in a modified single fibre myosin in vitro motility assay, in which an internal load (actin-binding protein) was added in different concentrations to evaluate the force-generating capacity. The force indices were the x-axis intercept and the slope of the relationship between the fraction of moving filaments and the α-actinin concentration. The force-generating capacity of the β/slow myosin isoform (type I) was weaker (P , 0.05) than the fast ...
Caldesmon interaction with smooth muscle myosin and its ability to cross-link actin filaments to myosin were investigated by the use of several bacterially expressed myosin-binding fragments of caldesmon. We have confirmed the presence of two functionally different myosin-binding sites located in domains 1 and 3/4a of caldesmon. The binding of the C-terminal site is highly sensitive to ionic strength and hardly participates in acto-myosin cross-linking, while the N-terminal binding site is relatively independent of ionic strength and apparently contains two separate myosin contact regions within residues 1-28 and 29-128 of chicken gizzard caldesmon. Both these N-terminal sub-sites are involved in the interaction with myosin and are predominantly responsible for the caldesmon-mediated high-affinity cross-linking of actin and myosin filaments, without affecting the affinity of direct acto-myosin interaction. Binding of caldesmon and its fragments to myosin or rod filaments revealed affinity in the ...
Mts1 protein (S100A4 according to a new classification) has been implicated in the formation of the metastatic phenotype via regulation of cell motility and invasiveness. Previously we have demonstrated that Mts1 protein interacted with the heavy chain of nonmuscle myosin in a calcium- dependent manner. To elucidate the role of the Mts1-myosin interaction, we mapped the Mts1-binding region on the myosin heavy chain molecule. We prepared proteolytically digested platelet myosin and a series of overlapped myosin heavy chain protein fragments and used them in a blot overlay with Mts1 protein. Here we report that the Mts1-binding site is located within a 29-amino acid region, at the C-terminal end of the myosin heavy chain (between 1909-1937 amino acids). Two-dimensional phosphopeptide analysis showed that Mts1 protein inhibits protein kinase C phosphorylation of the platelet myosin heavy chain at Ser-1917. We hypothesize that Mts1 protein regulates cytoskeletal dynamics of the metastatic cells ...
Contractile agonists can mobilize Ca2+ from both intracellular and extracellular stores in smooth muscle. This study addresses the role of Ca2+ mobilization as it relates to the complex manner by which Ca2+ regulates the contractile system in smooth muscle. In swine carotid media, both histamine and phenylephrine produced initial rapid increases in myosin phosphorylation and stress. Stress was sustained for the duration of the stimulus while myosin phosphorylation slowly declined to steady-state levels. Removal of extracellular Ca2+ or elimination of cellular Ca2+ influx did not dramatically reduce the initial rapid increase in myosin phosphorylation produced by either agonist but reduced steady-state levels of myosin phosphorylation to basal values. Initial rapid increases in stress were seen, but stress was not maintained. Following depletion of Ca2+ from sarcoplasmic reticulum, muscle activation by Ca2+ influx in the presence of phenylephrine occurred without an initial transient in myosin ...
TY - JOUR. T1 - Characterization of myosin V binding to brain vesicles. AU - Miller, Kyle E.. AU - Sheetz, Michael. PY - 2000/1/28. Y1 - 2000/1/28. N2 - Myosin II and V are important for the generation and segregation of subcellular compartments. We observed that vesicular myosin II and V were associated with the protein scaffolding of a common subset of vesicles by density sedimentation, electron microscopy, and immunofluorescence. Solubilization of either myosin II or V was caused by polyphosphates with the following efficacy at 10 mM: for myosin II ATP-Mg2+ = ATP = AMP-PNP (5- adenylyl imidodiphosphate) , pyrophosphate = tripolyphosphate ,, tetrapolyphosphate = ADP , cAMP = Mg2+; and for myosin V pyrophosphate = tripolyphosphate , ATP-Mg2+ = ATP = AMP-PNP ,, ADP = tetrapolyphosphate , cAMP = Mg2+. Consequently, we suggest solubilization was not an effect of phosphorylation, hydrolysis, or disassociation of myosin from actin filaments. Scatchard analysis of myosin V binding to stripped dense ...
1. Combined histochemical and biochemical single-fibre analyses [Staron & Pette (1987) Biochem. J. 243, 687-693], were used to investigate the rabbit tibialis-anterior fibre population. 2. This muscle is composed of four histochemically defined fibre types (I, IIC, IIA and IIB). 3. Type I fibres contain slow myosin light chains LC1s and LC2 and the slow myosin heavy chain HCI, and types IIA and IIB contain the fast myosin light chains LC1f, LC2f and LC3f and the fast heavy chains HCIIa and HCIIb respectively. 4. A small fraction of fibres (IIAB), histochemically intermediate between types IIA and IIB, contain the fast light myosin chains but display a coexistence of HCIIa and HCIIb. 5. Similarly to the soleus muscle, C fibres in the tibialis anterior muscle contain both fast and slow myosin light chains and heavy chains. The IIC fibres show a predominance of the fast forms and the IC fibres (histochemically intermediate between types I and IIC) a predominance of the slow forms. 6. A total of 60 ...
Title: Regulatory Light Chains of Striated Muscle Myosin. Structure, Function and Malfunction. VOLUME: 3 ISSUE: 2. Author(s):Danuta Szczesna-Cordary. Affiliation:Department of Molecular&Cellular Pharmacology, University of Miami School of MedicineRosenstiel Medical Sciences Building R-189, Room 6113, USA. Keywords:regulatory light chains of myosin (rlc), Phosphorylation, skinned fibers, familial hypertrophic, cardiomyopathy (fhc) mutations.. Abstract: Striated (skeletal and cardiac) muscle is activated by the binding of Ca2+ to troponin C and is regulated by the thin filament proteins, tropomyosin and troponin. Unlike in molluscan or smooth muscles, the myosin regulatory light chains (RLC) of striated muscles do not play a major regulatory role and their function is still not well understood. The N-terminal domain of RLC contains a Ca2+-Mg2+-binding site and, analogous to that of smooth muscle myosin, also contains a phosphorylation site. During muscle contraction, the increase in Ca2+ ...
TY - JOUR. T1 - Ca2+, cAMP, and changes in myosin phosphorylation during contraction of smooth muscle. AU - Aksoy, M. O.. AU - Mras, S.. AU - Kamm, K. E.. AU - Murphy, R. A.. PY - 1983. Y1 - 1983. N2 - Phosphorylation of myosin increases rapidly upon stimulation of an arterial smooth muscle. However, peak values are not maintained and phosphorylation declines, while active stress increases monotonically to a sustained steady state. The aim of this study was to determine the reason(s) for the transient change in myosin phosphorylation. Four hypotheses were considered: 1) reduced substrate, i.e., ATP depletion, 2) altered access of either the myosin kinase or phosphatase to the cross bridge, 3) reduced myosin kinase activity secondary to its phosphorylation by adenosine 3,5-cyclic monophosphate-dependent protein kinase, and 4) reduced myoplasmic [Ca2+] during the contraction. Our results suggest that the most likely explanation is that there are two Ca2+-dependent regulatory processes: 1) myosin ...
Antibodies with epitopes near the heavy meromyosin/light meromyosin junction distinguish the folded from the extended conformational states of smooth muscle myosin. Antibody 10S.1 has 100-fold higher avidity for folded than for extended myosin, while antibody S2.2 binds preferentially to the extended state. The properties of these antibodies provide direct evidence that the conformation of the rod is different in the folded than the extended monomeric state, and suggest that this perturbation may extend into the subfragment 2 region of the rod. Two antihead antibodies with epitopes on the heavy chain map at or near the head/rod junction. Magnesium greatly enhances the binding of these antibodies to myosin, showing that the conformation of the heavy chain in the neck region changes upon divalent cation binding to the regulatory light chain. Myosin assembly is also altered by antibody binding. Antibodies that bind to the central region of the rod block disassembly of filaments upon MgATP addition. ...
The global cell movements that shape an embryo are driven by intricate changes to the cytoarchitecture of individual cells. In a developing embryo, these changes are controlled by patterning genes that confer cell identity. However, little is known about how patterning genes influence cytoarchitecture to drive changes in cell shape. In this paper, we analyze the function of the folded gastrulation gene (fog), a known target of the patterning gene twist. Our analysis of fog function therefore illuminates a molecular pathway spanning all the way from patterning gene to physical change in cell shape. We show that secretion of Fog protein is apically polarized, making this the earliest polarized component of a pathway that ultimately drives myosin to the apical side of the cell. We demonstrate that fog is both necessary and sufficient to drive apical myosin localization through a mechanism involving activation of myosin contractility with actin. We determine that this contractility driven form of ...
In smooth muscle cells (SMCs) isolated from rabbit carotid, femoral, and saphenous arteries, relative myosin isoform mRNA levels were measured in RT-PCR to test for correlations between myosin isoform expression and unloaded shortening velocity. Unloaded shortening velocity and percent smooth muscle myosin heavy chain 2 (SM2) and myosin light chain 17b (MLC17b) mRNA levels were not significantly different in single SMCs isolated from the luminal and adluminal regions of the carotid media. Saphenous artery SMCs shortened significantly faster (P | 0.05) than femoral SMCs and had more SM2 mRNA (P | 0.05) than carotid SMCs and less MLC17b mRNA (P | 0.001) and higher tissue levels of SMB mRNA (P | 0.05) than carotid and femoral SMCs. No correlations were found between percent SM2 and percent MLC17b mRNA levels and unloaded shortening velocity in SMCs from these arteries. We have previously shown that myosin heavy chain (MHC) SM1/SM2 and SMA/SMB and MLC17a/MLC17b isoform mRNA levels correlate with protein
The last eukaryotic common ancestor already had an amazingly complex cell possessing genomic and cellular features such as spliceosomal introns, mitochondria, cilia-dependent motility, and a cytoskeleton together with several intracellular transport systems. In contrast to the microtubule-based dyneins and kinesins, the actin-filament associated myosins are considerably divergent in extant eukaryotes and a unifying picture of their evolution has not yet emerged. Here, we manually assembled and annotated 7852 myosins from 929 eukaryotes providing an unprecedented dense sequence and taxonomic sampling. For classification we complemented phylogenetic analyses with gene structure comparisons resulting in 79 distinct myosin classes. The intron pattern analysis and the taxonomic distribution of the classes suggest two myosins in the last eukaryotic common ancestor, a class-1 prototype and another myosin, which is most likely the ancestor of all other myosin classes. The sparse distribution of class-2 and
Although cytoskeletal proteins such as myosin II are implicated in the control of insulin secretion, their precise role is poorly understood. In other secretory cells, myosin II is predominantly regulated via the phosphorylation of the regulatory light chains (RLC). The current study was aimed at investigating RLC phosphorylation in beta-cells. In both the insulin-secreting cell line RINm5F and rat pancreatic islets, the RLC was basally phosphorylated on the myosin light chain kinase sites (Ser19/Thr18). Phosphorylation at these sites was not consistently increased by either metabolic stimuli (glyceraldehyde/glucose) or the depolarizing agent KCl. The RLC sites phosphorylated by protein kinase C (PKC) (Ser1/Ser2) were unphosphorylated in the basal state, not affected by nutrients or KCl, and only slightly increased by the PKC activator phorbol 12-myristate 13-acetate (PMA). Like the other insulin secretagogues, however, PMA did promote serine phosphorylation of the myosin heavy chain (MHC) in RINm5F
Centrosomes are the main microtubule (MT)-organizing centers in animal cells, but they also influence the actin/myosin cytoskeleton. The Drosophila CP190 protein is nuclear in interphase, interacts with centrosomes during mitosis, and binds to MTs directly in vitro. CP190 has an essential function in the nucleus as a chromatin insulator, but centrosomes and MTs appear unperturbed in Cp190 mutants. Thus, the centrosomal function of CP190, if any, is unclear. Here, we examine the function of CP190 in Cp190 mutant germline clone embryos. Mitosis is not perturbed in these embryos, but they fail in axial expansion, an actin/myosin-dependent process that distributes the nuclei along the anterior-to-posterior axis of the embryo. Myosin organization is disrupted in these embryos, but actin appears unaffected. Moreover, a constitutively activated form of the myosin regulatory light chain can rescue the axial expansion defect in mutant embryos, suggesting that CP190 acts upstream of myosin activation. A CP190
There are no specific protocols for Anti-Myosin Phosphatase 1+Myosin Phosphatase 2 antibody [YE336] (ab32519). Please download our general protocols booklet
Arterial vascular smooth muscle cells (VSMCs) play an important role in the function of many organ systems. Abnormality in the contractile and/or regulatory apparatus of smooth muscle is implicated in the pathogenesis of a variety of disease conditions such as hypertension, coronary and cerebral vasospasm, miscarriage, and erectile dysfunction. VSMCs in vivo show remarkable plasticity once they need to adapt to changes in environments, such as new development of vasculature and remodeling after vascular injury or during vascular diseases like arteriosclerosis (Owens, 1995). These arterial cells undergo rapid changes in shape and functional property from non-proliferative and contractile to proliferative and mobile phenotype.. Agonist stimulation of VSMCs induces phosphorylation of the 20 kDa regulatory light chain of myosin (MLC), which increases actin-activated myosin ATPase activity and contraction (Hartshorne, 1987; Somlyo and Somlyo, 2003). MLC phosphorylation is governed by the opposing ...
TY - JOUR. T1 - Myosin II is involved in the production of constitutive transport vesicles from the TGN. AU - Müsch, Anne. AU - Cohen, David. AU - Rodriguez-Boulan, Enrique. PY - 1997/7/28. Y1 - 1997/7/28. N2 - The participation of nonmuscle myosins in the transport of organelles and vesicular carriers along actin filaments has been documented. In contrast, there is no evidence for the involvement of myosins in the production of vesicles involved in membrane traffic. Here we show that the putative TGN coat protein p200 (Narula, N., I. McMorrow, G. Plopper, J. Doherty, K.S. Matlin, B. Burke, and J.L. Stow. 1992. J. Cell Biol. 114: 1113- 1124) is myosin II. The recruitment of myosin II to Golgi membranes is dependent on actin and is regulated by G proteins. Using an assay that studies the release of transport vesicles from the TGN in vitro we provide functional evidence that p200/myosin is involved in the assembly of basolateral transport vesicles carrying vesicular stomatitis virus G protein ...
Sheep polyclonal fast skeletal Myosin antibody validated for WB, IP, ELISA, IHC, Neut, ICC/IF and tested in Human, Mouse, Rat and Rabbit. Immunogen…
Toxoplasma gondii is an obligate intracellular parasite that enters cells by a process of active penetration. Host cell penetration and parasite motility are driven by a myosin motor complex consisting of four known proteins: TgMyoA, an unconventional Class XIV myosin; TgMLC1, a myosin light chain; and two membrane-associated proteins, TgGAP45 and TgGAP50. Little is known about how the activity of the myosin motor complex is regulated. Here, we show that treatment of parasites with a recently identified small-molecule inhibitor of invasion and motility results in a rapid and irreversible change in the electrophoretic mobility of TgMLC1. While the precise nature of the TgMLC1 modification has not yet been established, it was mapped to the peptide Val46-Arg59. To determine if the TgMLC1 modification is responsible for the motility defect observed in parasites after compound treatment, the activity of myosin motor complexes from control and compound-treated parasites was compared in an in vitro ...
Band 2 was identified as myosin heavy chain A (non-muscle) (Fig. 4B). Myosin heavy chain-A, non-muscle, is a cellular/cytoplasmic myosin very similar in structure to the skeletal, cardiac, and smooth muscle myosins. It has been identified in a wide range of cells including yeast and mammalian cells (22). The key feature of cytoplasmic myosin is its binding to actin filaments thereby generating contractile forces during cytokinesis and in maintaining cortical tension because of the hydrolysis of ATP. The function of cytoplasmic myosin is known to be regulated by its phosphorylation state (23). In Dictyostelium, for example, specific phosphorylation of threonine residues 1823, 1833, and 2029 is observed, which drives myosin from filamentous to a monomeric state thereby inhibiting cellular activity (24).. Tandem mass spectrometry was performed to confirm the identity of the protein migrating at 120 kDa in band 3. It was revealed to be drebrin 1 (F-actin-binding protein) (data not shown). It is an ...
© 2015 Elsevier Inc. Abstract We have investigated the effect of the E41K, R91G, and E139del β-tropomyosin (TM) mutations that cause congenital myopathy on the position of TM and orientation of actin monomers and myosin heads at different mimicked stages of the ATPase cycle in troponin-free ghost muscle fibers by polarized fluorimetry. A multi-step shifting of wild-type TM to the filament center accompanied by an increase in the amount of switched on actin monomers and the strongly bound myosin heads was observed during the ATPase cycle. The R91G mutation shifts TM further towards the inner and outer domains of actin at the strong- and weak-binding stages, respectively. The E139del mutation retains TM near the inner domains, while the E41K mutation captures it near the outer domains. The E41K and R91G mutations can induce the strong binding of myosin heads to actin, when TM is located near the outer domains. The E139del mutation inhibits the amount of strongly bound myosin heads throughout the ATPase
Cytokinesis is the process by which a cell partitions its surface and cytoplasm to form two daughter cells. In both animal and yeast cells, this process involves the assembly and contraction of an actomyosin ring. It is noteworthy that for a long time, among the hundreds of myosins known, only the conventional myosins of class II had been implicated in cell division (Field et al., 1999). However, a recent study established the involvement of two myosins of type V in S. pombe (Win et al., 2001). The asexual multiplication of T. gondii occurs by a peculiar process named endodyogeny, which is defined as the gradual development of two daughter parasites within a fully differentiated mother; the mother is incorporated into the daughters during the process (Fig. 1). In T. gondii, actin inhibitors did not prevent replication, per se, but disrupted the inheritance of mother cell organelles, resulting in the formation of residual bodies (Shaw et al., 2000). Therefore, myosin motor(s) were anticipated to ...
anti-Myosin Regulatory Light Chain 2, Smooth Muscle Isoform (MYL9) (pThr19), (AA 10-25) antibody (Cy5.5) ABIN753243 from antibodies-online
BACKGROUND: In contrast to conventional muscle myosins, where two different light chains (LCs) stabilize the elongated regulatory domain (RD) region of the head portion of the molecule, unconventional myosins are a diverse group of motors in which from one to six calmodulin (CaM) subunits are bound tandemly to the RD. In both cases, the heavy chains of the RDs have special sequences called IQ motifs to which the LCs or CaM bind. A previously puzzling aspect of certain unconventional myosins is their unusual mode of regulation, where activation of motility occurs at low levels of Ca2+. Although the atomic structure of the conventional muscle myosin RD has been determined, no crystallographic structure of the RD of an unconventional myosin is yet available. RESULTS: We have constructed a model of vertebrate CaM bound to the first IQ motif present in the neck region of an unconventional myosin (chicken brush border myosin I), using strict binding rules derived from the crystal structure of the ...
A monomeric myosin first spotted in electron micrographs almost 30 years ago has finally been united with a proposed function. Tyska and Mooseker (page 395) report that myosin-1A associates with and anchors a raft component in apical membranes.. Myosin-1A was previously thought to shuttle Golgi-derived cargos to the plasma membrane (after most of the distance had been covered using microtubule-based motors). But the in vitro evidence for this came from undifferentiated cells, and in mature, polarized colon epithelial cells, Tyska and Mooseker see no evidence of shuttling by myosin-1A. What they did spot was cofractionation and cross-linking of myosin-1A with the transmembrane disaccharidase sucrase-isomaltase (SI). This raft protein is lost from the apical surface when a fragment of either myosin-1A or SI interferes with the link between the two full-length proteins.. Thus, myosin-1A may serve as an anchor, with the clustering of SI in rafts helping to secure the link even if an individual ...
We studied the effect of chronic mechanical overloading on the isoenzyme composition of rat cardiac myosin in several experimental models: aortic stenosis (AS), aortic incompetence (AI), aortocaval fistula (ACF), overload of the non-infarcted area after left coronary ligation (INF), and overload of the spontaneously hypertensive rats (SHR). Samples of the left and right ventricles were isolated from these hearts, and myosins were analyzed by electrophoresis in non-dissociating conditions. The myosin isoenzymes were called V1, V2, and V3 in order of decreasing mobility, according to the nomenclature of Hoh et al. Controls of the Wistar and Wistar Kyoto (WKY) strains were almost exclusively V1, A slow age-dependent shift toward V3 was observed in the left ventricles of adult Wistar rats, which at 30 weeks of age (body weight 600 g) contained approximately 15% of this form. In all models of cardiac hypertrophy, an isoenzymic redistribution was observed with a significant increase in V3. The level ...
Define myosin. myosin synonyms, myosin pronunciation, myosin translation, English dictionary definition of myosin. n. Any of a class of proteins that bind with actin filaments and generate many kinds of cell movement, especially the contraction of myofibrils in muscle...
TY - JOUR. T1 - Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. AU - Espreafico, Enilza M.. AU - Cheney, Richard E.. AU - Matteoli, Michela. AU - Nascimento, Alexandra A C. AU - De Camilli, Pietro V.. AU - Larson, Roy E.. AU - Mooseker, Mark S.. PY - 1992/12. Y1 - 1992/12. N2 - Recent biochemical studies of p190, a calmodulin (CM)-binding protein purified from vertebrate brain, have demonstrated that this protein, purified as a complex with bound CM, shares a number of properties with myosins (Espindola, F. S., E. M. Espreafico, M. V. Coelho, A. R. Martins, F. R. C. Costa, M. S. Mooseker, and R. E. Larson. 1992. J. Cell Biol. 118:359-368). To determine whether or not p190 was a member of the myosin family of proteins, a set of overlapping cDNAs encoding the full-length protein sequence of chicken brain pi 90 was isolated and sequenced. Verification that the deduced primary structure was that of p190 was ...
Anti-Myosin VI polyclonal antibody (STJ96437) was developed using a synthesized peptide derived from the N-terminal region of human Myosin VI at AA range: 40-120. This antibody is applicable for use in western blot, immunohistochemistry-P, ELISA and immun
The actin cytoskeleton is crucial for function and morphology of neuronal synapses. Moreover, altered regulation of the neuronal actin cytoskeleton has been implicated in neuropsychiatric diseases such as autism spectrum disorder (ASD). Myosin XVI is a neuronally expressed unconventional myosin known to bind the WAVE regulatory complex (WRC), a regulator of filamentous actin (F-actin) polymerization. Notably, the gene encoding the myosins heavy chain (MYO16) shows genetic association with neuropsychiatric disorders including ASD. Here, we investigated whether myosin XVI plays a role for actin cytoskeleton regulation in the dendritic spines of cerebellar Purkinje cells (PCs), a neuronal cell type crucial for motor learning, social cognition and vocalization. We provide evidence that both myosin XVI and the WRC component WAVE1 localize to PC spines. Fluorescence recovery after photobleaching (FRAP) analysis of GFP-actin in cultured PCs shows that Myo16 knockout as well as PC-specific Myo16 knockdown,
Purification of native myosin filaments from muscle.: Analysis of the structure and function of native thick (myosin-containing) filaments of muscle has been ha
Results:. Patients with acute aortic dissection who presented within 3 hours after onset had elevated levels of circulating smooth-muscle myosin heavy-chain protein. In these patients, the assay had a sensitivity of 90.9%, a specificity of 98% compared with healthy volunteers, and a specificity of 83% compared with patients who had acute myocardial infarction; the clinical decision limit was 2.5 µg/L. All patients with proximal lesions had elevated levels of smooth-muscle myosin heavy-chain protein, and only patients with distal lesions had decreased levels (,2.5 µg/L). ...
Myosin-1, also known as striated muscle myosin heavy chain 1, is a protein that in humans is encoded by the MYH1 gene. This gene is most highly expressed in fast type IIX/D muscle fibres of vertebrates and encodes a protein found uniquely in striated muscle; it is a class II myosin with a long coiled coil tail that dimerizes and should not be confused with Myosin 1 encoded by the MYO1 family of genes (MYO1A-MYO1H). Class I MYO1 genes function in many cell types throughout biology and are single-headed membrane-binding myosins that lack a long coiled coil tail. Myosin is a major contractile protein that converts chemical energy into mechanical energy through the hydrolysis of ATP. Class II Myosins are hexameric proteins composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. Myosin heavy chains are encoded by a multigene family. In mammals, at least ten different myosin heavy chain (MYH) isoforms have been described from striated, smooth, but rarely in ...
The unconventional myosins form a large and diverse group of molecular motors. The number of known unconventional myosins is increasing rapidly and in the past year alone two new classes have been identified. Substantial progress has been made towards characterizing the properties and functions of t …
Muscle contraction involves the interaction of the myosin heads of the thick filaments with actin subunits of the thin filaments. Relaxation occurs when this interaction is blocked by molecular switches on these filaments. In many muscles, myosin-linked regulation involves phosphorylation of the myosin regulatory light chains (RLCs). Electron microscopy of vertebrate smooth muscle myosin molecules (regulated by phosphorylation) has provided insight into the relaxed structure, revealing that myosin is switched off by intramolecular interactions between its two heads, the free head and the blocked head. Three-dimensional reconstruction of frozen-hydrated specimens revealed that this asymmetric head interaction is also present in native thick filaments of tarantula striated muscle. Our goal in this study was to elucidate the structural features of the tarantula filament involved in phosphorylation-based regulation. A new reconstruction revealed intra- and intermolecular myosin interactions in ...
Myo15 encodes myosin XV (alternatively, Myosin XVa), a 3,511 amino acid member of the unconventional myosin family. Myosin XV has a proline-rich N-terminal extension that does not have sequence similarity to reported proteins and the function is unknown [Figure 3; amino acids 1-1200; SMART; (1-3)]. Myosin XV has a highly conserved motor domain (amino acids 1200-1884; NM_010862; SMART) following the N-terminal extension (2). The motor domain contains an adenosine triphosphate (ATP)- and an actin-binding site (amino acids 1299-1306 and 1776-1783, respectively; Uniprot) (4-6). The myosin neck region contains a variable number of light-chain binding (IQ) motifs (IQxxxRGxxxRK) and is linked to the motor domain by a converter region [(7); reviewed in (8;9)]. Myosin XV has two IQ motifs (amino acids 1909-1920; LQRCLRGFFIKR and amino acids 1932-1943; LQSRARGYLARQ) (5;8;9). The IQ motif is an α-helical structure that often mediates the binding of myosins to calmodulin, members of the EF-hand family of ...
Protein motors, such as kinesin and myosin, use chemical energy in the form of ATP to physically move along filaments and perform complex mechanical tasks in the cell, such as intracellular transport, cell division and muscle contraction. Myosin and kinesin are motor proteins that move along actin and microtubules, respectively. The primary goal for this dissertation research is to determine structure-function relationships in Myo I, a class-VII myosin, and in Ncd, a member of the kinesin superfamily. Myosin VII is a member of the myosin family that is found in human tissues and that has high homology to a D. discoideum myosin, Myo I. Work towards obtaining a crystal structure of Myo I are presented in this thesis. A Myo I structure would be the first structure of a class-VII myosin and a MyTH domain and would help discern the role myosin VIIs play in the cell. The structure of a different class of myosin may help better determine force-producing conformational changes in myosins. Ncd is a ...
Protein motors, such as kinesin and myosin, use chemical energy in the form of ATP to physically move along filaments and perform complex mechanical tasks in the cell, such as intracellular transport, cell division and muscle contraction. Myosin and kinesin are motor proteins that move along actin and microtubules, respectively. The primary goal for this dissertation research is to determine structure-function relationships in Myo I, a class-VII myosin, and in Ncd, a member of the kinesin superfamily. Myosin VII is a member of the myosin family that is found in human tissues and that has high homology to a D. discoideum myosin, Myo I. Work towards obtaining a crystal structure of Myo I are presented in this thesis. A Myo I structure would be the first structure of a class-VII myosin and a MyTH domain and would help discern the role myosin VIIs play in the cell. The structure of a different class of myosin may help better determine force-producing conformational changes in myosins. Ncd is a ...
Abstract: Studies in Dictyostelium discoideum have established that the cycle of myosin II bipolar filament assembly and disassembly controls the temporal and spatial localization of myosin II during critical cellular processes, such as cytokinesis and cell locomotion. Myosin heavy chain kinase A (MHCK A) is a key enzyme regulating myosin II filament disassembly through myosin heavy chain phosphorylation in Dictyostelium. Under various cellular conditions, MHCK A is recruited to actin-rich cortical sites and is preferentially enriched at sites of pseudopod formation, and thus MHCK A is proposed to play a role in regulating localized disassembly of myosin II filaments in the cell. MHCK A possesses an aminoterminal coiled-coil domain that participates in the oligomerization, cellular localization, and actin binding activities of the kinase. In the current study, we show that the interaction between the coiled-coil domain of MHCK A and filamentous actin leads to an ~40-fold increase in the initial ...
Abstract: Myosin heavy chain kinase (MHCK) A phosphorylates mapped sites at the C-terminal tail of Dictyostelium myosin II heavy chain, driving disassembly of myosin filaments both in vitro and in vivo. MHCK A is organized into three functional domains that include an N-terminal coiled-coil region, a central kinase catalytic domain unrelated to conventional protein kinases, and a WD repeat domain at the C terminus. MHCK B is a homologue of MHCK A that possesses structurally related catalytic and WD repeat domains. In the current study, we explored the role of the WD repeat domains in defining the activities of both MHCK A and MHCK B using recombinant bacterially expressed truncations of these kinases either with or without their WD repeat domains. We demonstrate that substrate targeting is a conserved function of the WD repeat domains of both MHCK A and MHCK B and that this targeting is specific forDictyostelium myosin II filaments. We also show that the mechanism of targeting involves direct ...
TY - JOUR. T1 - Movement of myosin‐coated structures on actin cables. AU - Sheetz, Michael. AU - Spudich, James A.. PY - 1983/1/1. Y1 - 1983/1/1. N2 - Myosin‐coated spheres from 0.6 to 120 μm in diameter move in vitro on a substratum of polar arrays of actin cables derived from the alga Nitella. The force for this movement is provided by skeletal muscle myosin since it is ATP‐dependent, and N‐ethylmaleimide (NEM) inactivation of the myosin blocks movement. These observations demonstrate that attachment of myosin in a random orientation to structures will enable those structures to move along polar arrays of actin filaments.. AB - Myosin‐coated spheres from 0.6 to 120 μm in diameter move in vitro on a substratum of polar arrays of actin cables derived from the alga Nitella. The force for this movement is provided by skeletal muscle myosin since it is ATP‐dependent, and N‐ethylmaleimide (NEM) inactivation of the myosin blocks movement. These observations demonstrate that attachment ...
Blebbistatin is a small-molecule, high-affinity, noncompetitive inhibitor of myosin II. We have used negative staining electron microscopy to study the effects of blebbistatin on the organization of the myosin heads on muscle thick filaments. Loss of ADP and Pi from the heads causes thick filaments to lose their helical ordering. In the presence of 100 microM blebbistatin, disordering was at least 10 times slower. In the M.ADP state, myosin heads are also disordered. When blebbistatin was added to M.ADP thick filaments, helical ordering was restored. However, blebbistatin did not improve the order of thick filaments lacking bound nucleotide. Addition of calcium to relaxed muscle homogenates induced thick-thin filament interaction and filament sliding. In the presence of blebbistatin, filament interaction was inhibited. These structural observations support the conclusion, based on biochemical studies, that blebbistatin inhibits myosin ATPase and actin interaction by stabilizing the closed switch 2
Viruses are obligatory parasites that depend on host Hula o for their replication as el as for their local and syst movement to establish infection. Although myosin motors are hought to contribute to plant virus infection, their exact role in the specific infection steps have not been addressed. Here we investigated the replication, cell-to-cell and systemic spread of Tobacco mosaic virus (TMV) using dominant negative inhibition of myosin activity. We found that interference with the functions of three class VIII myosins and two class XI myosins significantly reduced the local and long-distance transport o virus. We further determined that the inactivation of myosins XI-2 and XI-K affected the structure and dynamic behavior of th ER leading to aggregation of he viral movement protein (MP) and to a delay in the MP accumulation in plasmodesmata (PD) The inactivation of myosin XI-2 but not of myosin XI-K affected the localization pattern of the 126k replicase subunit and the level of TMV ...
Non-muscle cells express multiple myosin-II electric motor necessary protein myosin IIA, myosin IIB and myosin IIC transcribed from different loci in the individual genome. the dispersing margins had KU14R manufacture been dropped in myosin II? cells. Amazingly, myosin IIcells displayed longer actin filaments connected to focal connections in the scattering margins parallel. Hence, with different assignments in the regulations of the actin network and focal connections development, both myosin IIB and IIA determine the fate of lamellipodia extension during cell spreading. Launch Cell migration has a fundamental function in the maintenance and advancement of the regular physiology of every patient. Deregulation of cell migration is normally suggested as a factor in cancers spread, mental retardation, an infection, and vascular illnesses. Cells initiate migration by increasing their plasma membrane layer in the type of lamellipodia that needs the orchestration of the cell cytoskeleton [1]. KU14R ...
Myosin: Biosynthesis, Classes and Function opens with a discussion on class I myosins, the most varied members of the myosin superfamily and a remarkable group of molecular motor proteins that move actin filaments and produce force. Class I myosin molecules have various physiological roles including maintenance of normal intestinal brush border structure, glucose homeostasis, glomerular filtration, immune function, and tumor promotion and suppression, and new studies are revealing that mutations may lead to diseases including cancer and kidney disease. Thus, the authors review the structure and function of the eight myosin-I isoforms (Myo1a-Myo1h) that are expressed in mammals. Next, the book discusses muscle contractile function and its association with the activity of the protein complex actomyosin, in which myosin exhibits enzyme activity, namely the ability to hydrolyze ATP.. The demonstrated ability of calix[4]arenes C-97, C-99, C-90 and thiacalix[4]arenes C-798 and C-800 can be used for ...
Cardiac-specific myosin light chain kinase (cMLCK) is the kinase predominantly responsible for the maintenance of the basal level of phosphorylation of cardiac myosin light chain 2 (MLC2), which it phosphorylates at Ser-15. This phosphorylation repels the myosin heads from the thick myosin filament and moves them toward the thin actin filament. Unlike smooth muscle cells, MLC2 phosphorylation in striated muscle cells appears to be a positive modulator of Ca2+ sensitivity that shifts the Ca2+-force relationship toward the left and increases the maximal force response and thus does not initiate muscle contraction. Recent studies have revealed an increasing number of details of the biochemical, physiological, and pathophysiological characteristics of cMLCK. The combination of recent technological advances and the discovery of a novel class of biologically active nonstandard peptides will hopefully translate into the development of drugs for the treatment of heart diseases. (Circ J 2013; 77: ...
TY - JOUR. T1 - Effects of the myosin ATPase inhibitor, 2,3-butanedione-2-monoxime, on growth and dimorphic switches of Candida albicans. AU - Woo, M.. AU - Jwa, M.. AU - Kim, J.. AU - Song, K.. PY - 2000/1/1. Y1 - 2000/1/1. N2 - Dimorphic yeast Candida albicans reversibly switches between the form of yeast and hyphae depending on external conditions. We investigated possible roles of the myosin family in the growth and dimorphic switches of C. albicans with a general myosin ATPase inhibitor, 2,3-butanedione-2-monoxime (BDM). Transition to hyphae as well as proliferation by budding was completely inhibited by BDM at 16 mM. Presence of 16 mM BDM did not affect hyphae-to-bud transition but it blocked budding. The effects of BDM on yeast growth and dimorphic switches were reversible. More than 70% of the BDM-treated cells demonstrated defects in the amount and the polarized localization of F-actin as well as in the shape and migration of the nucleus, suggesting that myosin activities are needed in ...
TY - JOUR. T1 - Bio-nanomuscle project. T2 - Contractile properties of single actin filaments in an a-band motility assay system. AU - Suzuki, Madoka. AU - Fujita, Hideaki. AU - Ishiwata, Shinichi. PY - 2004. Y1 - 2004. N2 - We have developed a new microscopic technique to measure the force generated on a single actin filament (FA) in the A-band in which the intact lattice structure composed of myosin thick filaments is maintained; we call this newly developed system Bionanomuscle (or an A-band motility assay system). The A-bands were prepared by selective removal of thin filaments from rabbit skeletal glycerinated myofibrils under optical microscope with the use of gelsolin (a severing and barbed (B)-end capping protein of FA) that was prepared from bovine serum. A polystyrene bead of 1 μm in diameter attached to the B-end of FA (through a gelsolin molecule attached to the surface of the bead) was trapped and manipulated with optical tweezers. The displacement of the bead up to 200 nm ...
Myosin IIIA is a protein that in humans is encoded by the MYO3A gene.[1][2] The protein encoded by this gene belongs to the myosin superfamily. Myosins are actin-dependent motor proteins and are categorized into conventional myosins (class II) and unconventional myosins (classes I and III through XV) based on their variable C-terminal cargo-binding domains. Class III myosins, such as this one, have a kinase domain N-terminal to the conserved N-terminal motor domains and are expressed in photoreceptors. The protein encoded by this gene plays an important role in hearing in humans. Three different recessive, loss of function mutations in the encoded protein have been shown to cause nonsyndromic progressive hearing loss. Expression of this gene is highly restricted, with the strongest expression in retina and cochlea.[2] ...
Fig 1 Positions of subdomains and connectors in the three myosin states and closure of the 50-kDa cleft. a, A comparison of the myosin V motor domain to the Dictyostelium myosin II in the near-rigor and transition states shows the different positions of the subdomains, nucleotide-binding elements and connectors in each state. The structures have been superimposed on the N-terminal subdomains. Relative to this subdomain, the rotation necessary to move from the myosin V state to the near-rigor state is indicated for each subdomain of myosin V; similarly, the rotation necessary to move from the near-rigor to the transition state is indicated on the subdomains of the transition-state structure. Contours of the solvent-accessible cavities for the near-rigor (1,735 ...
SILVA, A C R; KENDRICK-JONES, J; REINACH, Fernando de Castro. Construction of a regulatory myosin light chain capable regulation of myosin. Arquivos de Biologia e Tecnologia[S.l: s.n.], 1988 ...
Looking for online definition of myosin, heavy polypeptide 5 in the Medical Dictionary? myosin, heavy polypeptide 5 explanation free. What is myosin, heavy polypeptide 5? Meaning of myosin, heavy polypeptide 5 medical term. What does myosin, heavy polypeptide 5 mean?
This study illuminates the aspects of cell migration, which is central to many biological processes. To understand cell migration we examine the relationship between local cytoskeletal features and local morphology. We demonstrate this relationship on cells stained for Actin and Myosin We connect the actin/myosin co-localizated structural organization to movements such as membrane protrusions. Membrane protrusions are good indicators of cell migration. Cells can sense the mechanical stiffness or the chemical identity of the surfaces they attach to. We show that these surfaces impact cytoskeletal structure. We develop a classifier to correlate the contextual features extracted from actin/myosin co-localized structure to different cell surfaces. We also describe a new distance based metric to measure the strength of collocated multi-channel two dimensional data for user selected regions. We provide tools, implemented as plugins for the popular ImageJ toolkit, that are available for download by the ...
Both smooth muscle and nonmuscle myosin II activity is regulated by the phosphorylation state of the myosin regulatory light chain (MLC, MRLC, MLC20, Myl9). Phosphorylation of MLC at Thr-18 and Ser-19 activates myosin II motor activity and increases myosin filament stability. This activation has important roles in vari
As shown in this study, Myo1c is one of the main class I myosins expressed in B cells. Previous observations from our group indicated that this molecule could be involved in cytoskeleton rearrangements of B lymphocytes, during the spreading induced by immobilized anti-CD44, B220, or MHC-II Abs (17). During live-cell observations using GFP tagged Myo1c, we observed strong localization of this molecule in all membrane protrusions generated during spreading in addition to enrichment of the protein at the points where membrane extensions begin to appear.. Class I myosins have been identified recently as key players in regulating cell deformation (28). Although overexpression of full-length Myo1c did not significantly alter the cell morphology; when endogenous myosin function is altered by using the dominant negative IQ-Tail construct, the spreading process is modified. The pictures show a nonpolarized spreading pattern, which means that the cells do not produce one or two long projections as control ...
Four Caenorhabditis elegans genes encode muscle-type specific myosin heavy chain isoforms: myo-1 and myo-2 are expressed in the pharyngeal muscles; unc-54 and myo-3 are expressed in body wall muscles. We have used transformation-rescue and lacZ fusion assays to determine sequence requirements for regulated myosin gene expression during development. Multiple tissue-specific activation elements are present for all four genes. For each of the four genes, sequences upstream of the coding region are tissue-specific promoters, as shown by their ability to drive expression of a reporter gene (lacZ) in the appropriate muscle type. Each gene contains at least one additional tissue-specific regulatory element, as defined by the ability to enhance expression of a heterologous promoter in the appropriate muscle type. In rescue experiments with unc-54, two further requirements apparently independent of tissue specificity were found: sequences within the 3 non-coding region are essential for activity while ...
Myosin regulatory light polypeptide 9 is a protein that in humans is encoded by the MYL9 gene. Myosin, a structural component of muscle, consists of two heavy chains and four light chains. The protein encoded by this gene is a myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads. The encoded protein binds calcium and is activated by myosin light chain kinase. Two transcript variants encoding different isoforms have been found for this gene. GRCh38: Ensembl release 89: ENSG00000101335 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000067818 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed Reference:. Kumar CC, Mohan SR, Zavodny PJ, Narula SK, Leibowitz PJ (May 1989). Characterization and differential expression of human vascular smooth muscle myosin light chain 2 isoform in nonmuscle cells. Biochemistry. 28 (9): 4027-35. doi:10.1021/bi00435a059. PMID 2526655. Entrez Gene: myosin. Stelzl U, Worm U, Lalowski M, et al. ...
TY - JOUR. T1 - Involvement of headless myosin X in the motility of immortalized gonadotropin-releasing hormone neuronal cells. AU - Wang, Jun Jie. AU - Fu, Xiu Qing. AU - Guo, Yu Guang. AU - Yuan, Lin. AU - Gao, Qian Qian. AU - Yu, Hua Li. AU - Shi, Heng Liang. AU - Wang, Xing Zhi. AU - Xiong, Wen Cheng. AU - Zhu, Xiao Juan. N1 - Funding Information: This work was supported by the National Natural Science Foundation of China (30670689) and the Program for New Century Excellent Talents in University (NCET-07-0173), Specialized Research Fund for the Doctoral Program of High Education (20060200008) and Scientific Research Foundation for the Returned Overseas Chinese Scholars from the Ministry of Education of China.. PY - 2009/5. Y1 - 2009/5. N2 - Myosin X (Myo X), an unconventional myosin with a tail homology 4-band 4.1/ezrin/radixin/moesin (MyTH4-FERM) tail, is expressed ubiquitously in various mammalian tissues. In addition to the full-length Myo X (Myo X FL), a headless form is synthesized in ...
The actomyosin network is thought to support fundamental processes of plant development and cell expansion such as polarized elongation of root hairs and the diffuse growth of epidermal and mesophyll cells. Inhibition of myosins via pharmacological treatments represents one of the key approaches for understanding of their roles in different cellular processes. However, the use of the standard plant myosin inhibitor, 2,3-butanedionemonoxime (BDM), is questioned as it requires a high concentration and may not be as specific as desired. By testing drugs that inhibit animal and yeast myosins V, the Staiger laboratory previously found pentabromopseudilin (PBP) as a potential inhibitor of plant myosins in vivo. In order to verify PBP as a plant myosin inhibitor in vitro, an actin filament gliding assay powered by chicken Myosin Va (MyoVa) was developed as a positive control using Total Internal Reflection Fluorescence Microscopy (TIRFM). Here, we partially purified a YFP-tagged Myosin XIK from Arabidopsis
TY - JOUR. T1 - Dynamic regulation of vascular myosin light chain (MYL9) with injury and aging. AU - Shehadeh, Lina A.. AU - Webster, Keith A.. AU - Hare, Joshua M.. AU - Vazquez-Padron, Roberto I.. N1 - Copyright: Copyright 2012 Elsevier B.V., All rights reserved.. PY - 2011/10/7. Y1 - 2011/10/7. N2 - Background: Aging-associated changes in the cardiovascular system increase the risk for disease development and lead to profound alterations in vascular reactivity and stiffness. Elucidating the molecular response of arteries to injury and age will help understand the exaggerated remodeling of aging vessels. Methodology/Principal Findings: We studied the gene expression profile in a model of mechanical vascular injury in the iliac artery of aging (22 months old) and young rats (4 months old). We investigated aging-related variations in gene expression at 30 min, 3 d and 7 d post injury. We found that the Myosin Light Chain gene (MYL9) was the only gene differentially expressed in the aged versus ...
The development of cell-cell junctions was a fundamental step in metazoan evolution and human health depends on the formation and function of cell junctions. the apical junction and an apically-directed actin flow generated by NMII contraction.45 As a major force generator and component of adherens junctions NMII may also have yet to be discovered roles at the junction. Myo1e at Specialized Glomerular Junctional Complexes Class I myosins are single-headed motors with short tails that bind to lipid membranes.46 They are phylogenetically ancient and are found in amoebae fungi and animals. Many organisms express several class I myosins; the slime mold expresses seven46 and humans express eight class I myosins.3 Myo1a one of the best known class I myosins forms a link between the plasma membrane and the actin filaments of intestinal microvilli.47 Myo1e (initially called human myosin-1c or myr3) has a longer tail that contains both a membrane-binding domain and an SH3 domain48 (Fig.?1). Myo1e is ...
Phosphorylation of the regulatory light chain of myosin II (MLC(20)) at the activation sites promotes both the motor activity and the filament formation of myosin II, thus playing an important role in various cell motile processes. In contrast, the physiological function of phosphorylation of MLC(20) at the inhibitory sites is unknown. Here we report for the first time the function of the inhibitory site phosphorylation in the cells. We successfully produced the antibodies specifically recognizing the phosphorylation sites of MLC(20) at Ser1, and the platelet-derived growth factor (PDGF)-induced change in the phosphorylation at the Ser1 was monitored. The phosphorylation of MLC(20) at the Ser1 significantly increased during the PDGF-induced actin cytoskeletal reorganization. PDGF disassembled the stress fibers, and this was attenuated with the expression of unphosphorylatable MLC(20) at the Ser1/Ser2 phosphorylation sites. The present results suggest that the down-regulation of myosin II activity
TY - JOUR. T1 - Myosin II contributes to cell-scale actin network treadmilling through network disassembly. AU - Wilson, Cyrus A.. AU - Tsuchida, Mark A.. AU - Allen, Greg M.. AU - Barnhart, Erin L.. AU - Applegate, Kathryn T.. AU - Yam, Patricia T.. AU - Ji, Lin. AU - Keren, Kinneret. AU - Danuser, Gaudenz. AU - Theriot, Julie A.. PY - 2010/5/20. Y1 - 2010/5/20. N2 - Crawling locomotion of eukaryotic cells is achieved by a process dependent on the actin cytoskeleton: protrusion of the leading edge requires assembly of a network of actin filaments, which must be disassembled at the cell rear for sustained motility. Although ADF/cofilin proteins have been shown to contribute to actin disassembly, it is not clear how activity of these locally acting proteins could be coordinated over the distance scale of the whole cell. Here we show that non-muscle myosin II has a direct role in actin network disassembly in crawling cells. In fish keratocytes undergoing motility, myosin II is concentrated in ...
To characterize the structure of jaw muscle fibres expressing masticatory (superfast) myosin, X-ray diffraction patterns of glycerinated fibres of dog masseter were compared with those of dog tibialis anterior in the relaxed state. Meridional reflections of masseter fibres were laterally broad, indicating that myosin filaments are staggered along the filament axis. Compared with tibialis anterior fibres, the peak of the first myosin layer line of masseter fibres was lower in intensity and shifted towards the meridian, while lattice spacings were larger at a similar sarcomere length. These suggest that the myosin heads of masticatory fibres are mobile, and tend to protrude from the filament shaft towards actin filaments. Lowering temperature or treating with N-phenylmaleimide shifted the peak of the first myosin layer line of tibialis anterior fibres towards the meridian and the resulting profile resembled that of masseter fibres. This suggests that the protruding mobile heads in the non-treated ...
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Cell division concludes with cytokinesis, a process driven by a contractile ring of actin and myosin that lies underneath the plasma membrane at the cells equator. Although myosin is essential for cytokinesis in various animal models, whether and to what extent this reflects its motor activity or its ability to crosslink actin has been a matter of debate. Now Daniel Osorio, Ana Carvalho and colleagues tackle this problem with the help of CRISPR/Cas9 gene editing and C. elegans embryos. Mutations introduced into the ATPase domain of non-muscle myosin-2 (NMY-2, the sole myosin required for early cytokinesis) bind to actin but fail to translocate it in vitro. In the animal, these motor-dead mutations lead to adult sterility and embryonic inviability, and fail to support cytokinesis. When motor activity is partially impaired, cytokinesis is prolonged and more sensitive to reductions in overall NMY-2 levels. Finally, although actin levels in the contractile ring are not affected by either NMY-2 ...
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Functional characteristics of Myosin V and Broad Complex during Drosophila oogenesis identification and analysis of myosin genes in Drosophila ...
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MMIb; MMI-beta; Myo1C isoform B; myr2; NM1; NMI Nuclear myosin I (NM1) belongs to the group of class I myosins, which are monomeric, nonprocessive, slow-rate, and low-duty ratio molecular motors...
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体[NOQ7.5.4D](ab11083)可与小鼠, 大鼠, 羊, 兔, 山羊, 鸡, 豚鼠, 仓鼠等样本反应并经WB, ELISA, IHC, RIA, EM…
Slow Skeletal Myosin Heavy chain小鼠单克隆抗体可与小鼠, 大鼠, 鸡, 人样本反应并经WB, ELISA, IHC, ICC/IF实验严格验证,被1篇文献引用。
TY - JOUR. T1 - Unidirectional Brownian motion observed in an in silico single molecule experiment of an actomyosin motor. AU - Takano, Mitsunori. AU - Terada, Tomoki P.. AU - Sasai, Masaki. PY - 2010/4/27. Y1 - 2010/4/27. N2 - The actomyosin molecular motor, the motor composed of myosin II and actin filament, is responsible for muscle contraction, converting chemical energy into mechanical work. Although recent single molecule and structural studies have shed new light on the energy-converting mechanism, the physical basis of the molecular-level mechanism remains unclear because of the experimental limitations. To provide a clue to resolve the controversy between the lever-arm mechanism and the Brownian ratchet-like mechanism, we here report an in silico single molecule experiment of an actomyosin motor.When we placed myosin on an actin filament and allowed myosin to move along the filament, we found that myosin exhibits a unidirectional Brownian motion along the filament. This ...
Excitation-contraction coupling of smooth muscle refers to a chain of coupled physiological processes which convert a stimulus to a mechanical response. These processes can be disassociated into ionic transport during cell membrane excitation, activation of myosin light chains, and muscle contraction caused by actin-myosin interaction (filament sliding). This thesis concerns the development of a framework which allows to model the smooth muscle excitation-contraction coupling constitutively by applying the principle of virtual power and dissipation inequality. In doing so, the transport of ions through membrane channels is characterized by an ionic flux and an ionic supply, both governed by an electrochemical potential energy. By letting the Helmholtz free energy to be dependent on the myosin light chain configurations during contraction, the myosin light chain activation process, i.e., myosin phosphorylation, is included. The activation process links the membrane excitation to the filament ...
Myosin specificity[edit]. Blebbistatin is a potent inhibitor of nonmuscle myosin IIA and IIB, cardiac myosin, skeletal myosin ... nonmuscle myosin-2 oocyte cytokinesis effective at 300 μM[33] C. elegans nonmuscle myosin-2 acto-myosin colocalization ... myosin isoform or muscle type assay type IC50 Dictyostelium discoideum myosin II motor domain basal ATPase 2.96 ± 0.45 μM,[7] ... It is widely used in research to inhibit heart muscle myosin, non-muscle myosin II, and skeletal muscle myosin. Blebbistatin ...
She chose the motor protein myosin as the topic of her Ph.D. work in the laboratories of Mark Mooseker and Peter Novick at Yale ... She developed a modified in vitro motility assay to show that both Myo2p and Myo4p class V myosins in yeast appear to be non- ... Reck-Peterson, S. L.; Tyska, M. J.; Novick, P. J.; Mooseker, M. S. (2001-05-28). "The yeast class V myosins, Myo2p and Myo4p, ... Her work focused on the class V myosins, which have multiple functions in the cell ranging from mRNA transport to cell polarity ...
Kruppa AJ, Kendrick-Jones J, Buss F (2016). "Myosins, Actin and Autophagy". Traffic. 17 (8): 878-90. doi:10.1111/tra.12410. PMC ...
Kruppa AJ, Kendrick-Jones J, Buss F (2016). "Myosins, Actin and Autophagy". Traffic (Copenhagen, Denmark). 17 (8): 878-90. doi: ...
Myosin motoring along F-actin filaments generates contractile forces in so-called actomyosin fibers, both in muscle as well as ... They also act as tracks for the movement of myosin molecules that affix to the microfilament and "walk" along them. In general ... Actin structures are controlled by the Rho family of small GTP-binding proteins such as Rho itself for contractile acto-myosin ... Cooper, Geoffrey M. (2000). "Actin, Myosin, and Cell Movement". The Cell: A Molecular Approach. 2nd Edition. Archived from the ...
Myosin regulatory light polypeptide 9 is a protein that in humans is encoded by the MYL9 gene. Myosin, a structural component ... "Entrez Gene: myosin". Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for ... The protein encoded by this gene is a myosin light chain that may regulate muscle contraction by modulating the ATPase activity ... Higashihara M, Watanabe M, Usuda S, Miyazaki K (2008). "Smooth muscle type isoform of 20 kDa myosin light chain is expressed in ...
Myosin fought back before Chiswick Bridge to reduce the deficit, but Actin won by around two lengths. Oxford's men's trial race ... The CUWBC president, Larkin Sayre, rowed in Myosin who lost the toss and were on the Middlesex side of the river. The race was ... As such the boats were named Actin and Myosin, the proteins which make the two muscle fibres that pull against each other in ... "CUWBC: Actin vs Myosin". The Boat Race Company Limited. 16 December 2019. Retrieved 10 January 2020. "OUBC Trial Eights Crews ...
Interactions between actin, myosin and an actin-binding protein from rabbit alveolar macrophages. Alveolar macrophage myosin ... Interactions of actin, myosin and a new actin-binding protein of rabbit pulmonary macrophages II. Role in cytoplasmic movement ... Interactions of actin, myosin and an actin-binding protein of rabbit pulmonary macrophages III. Effects of cytochalasin B. J ... Interactions of actin, myosin and an actin-binding protein of chronic myelogenous leukemia leukocytes. J Clin Invest. 1976; 57: ...
Hodge T, Cope MJ (October 2000). "A myosin family tree". Journal of Cell Science. 113 (19): 3353-4. PMID 10984423. Mount DM ( ...
Filamin B, beta (FLNB), also known as Filamin B, beta (actin binding protein 278), is a cytoplasmic protein which in humans is encoded by the FLNB gene. FLNB regulates intracellular communication and signalling by cross-linking the protein actin to allow direct communication between the cell membrane and cytoskeletal network, to control and guide proper skeletal development.[5] Mutations in the FLNB gene are involved in several lethal bone dysplasias, including boomerang dysplasia and atelosteogenesis type I.[6][7][8] ...
The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests they are regulated by a number of different stimuli, and interact with multiple proteins. These proteins, directly or indirectly, associate with the small GTPase CDC42, known to regulate formation of actin filaments, and the cytoskeletal organising complex, Arp2/3. The WASp family proteins includes WASp, N-WASp, SCAR/WAVE, WHAMM and WASH the five of them share a C- terminal VCA (verprolin, central, acidic) domain where they interact with actin nucleating complex (ARP2/3) and they differ in their terminal domains. WASp and N-WASP are analogs, they contain an N-terminal EVH1 domain, a C-terminal VCA domain and central B and GBD (GTP binding domain) domains. WASp, is expressed exclusively in hematopoietic cells and neuronal WASp (N-WASp), is ubiquitously ...
neuroaxonal damage is the pathological substrate of permanent disability in various neurological disorders. ... Here, we review what is known about the structure and function of neurofilaments, discuss analytical aspects and knowledge of age-dependent normal ranges of neurofilaments and provide a comprehensive overview of studies on neurofilament light chain as a marker of axonal injury in different neurological disorders, including multiple sclerosis, neurodegenerative dementia, stroke, traumatic brain injury, amyotrophic lateral sclerosis and Parkinson disease ...
Each thick filament is approximately 15 nm in diameter, and each is made of several hundred molecules of myosin. A myosin ... The filaments of actin and myosin then form linkages. After binding, myosin pulls actin filaments toward each other, or inward ... Half of the myosin heads angle to the left and half of them angle to the right, creating an area in the middle of the filament ... Myofilaments are the filaments of myofibrils, constructed from proteins,[1] principally myosin or actin. Types of muscle are ...
Myosin-9 also known as myosin, heavy chain 9, non-muscle or non-muscle myosin heavy chain IIa (NMMHC-IIA) is a protein which in ... myosin II filament. • cell cortex. • brush border. • actomyosin. • myosin complex. • integrin complex. • ruffle. • cell nucleus ... Myosin IIs are motor proteins that are part of a superfamily composed of more than 30 classes.[7][8][9] Class II myosins ... The path to myosin filament formation, which is shared by NM II and smooth muscle myosin, starts with a folded inactive ...
In mammals talin-1 is ubiquitously expressed; talin-1 is found complexed to integrins and localized to intercalated discs of cardiac muscle and to costamere structures of both skeletal and cardiac muscles,[32] in correspondence with the I-band and M-line.[33][34][35] Talin-1 is also found at focal adhesions of smooth muscle cells [36] and non-muscle cells.[9] In undifferentiated cultures of myoblasts, talin-1 expression is perinuclear, and then progresses to a cytoplasmic distribution followed by a sarcomlemmal, costameric-like pattern by day 15 of differentiation.[37] Homozygous disruption of TLN1 in mice is embryonic lethal, demonstrating that talin-1 is required for normal embryogenesis.[38] It has been shown, however, that talin-1 expression is minor in adult cardiomyocytes, and becomes more prominent at costameres during cardiac hypertrophy induced by pharmacological and mechanical stress.[39] The primary function of talin-1 involves the linkage of integrins to the actin cytoskeleton and in ...
Cytoplasmic dynein, which has a molecular mass of about 1.5 megadaltons (MDa), is a dimer of dimers, containing approximately twelve polypeptide subunits: two identical "heavy chains", 520 kDa in mass, which contain the ATPase activity and are thus responsible for generating movement along the microtubule; two 74 kDa intermediate chains which are believed to anchor the dynein to its cargo; two 53-59 kDa light intermediate chains; and several light chains. The force-generating ATPase activity of each dynein heavy chain is located in its large doughnut-shaped "head", which is related to other AAA proteins, while two projections from the head connect it to other cytoplasmic structures. One projection, the coiled-coil stalk, binds to and "walks" along the surface of the microtubule via a repeated cycle of detachment and reattachment. The other projection, the extended tail, binds to the light intermediate, intermediate and light chain subunits which attach dynein to its cargo. The alternating ...
The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, NMR.[1] The secondary and tertiary structures of destrin are similar to the gelsolin family which is another actin-regulating protein family. There are three ordered layers to destrin which is a globular protein. There is a central β sheet that is composed of one parallel strand and three antiparallel strands. This β sheet is between a long α helix along with a shorter one and two shorter helices on the opposite side. The four helices are parallel to the β strands.[1] ...
Ankyrin-B is a member of the ankyrin family of proteins. ankyrin-1 has shown to be essential in normal function of erythrocytes;[10] however, ankyrin-B and ankyrin-3 play essential roles in the localization and membrane stabilization of ion transporters and ion channels in cardiomyocytes.[9][11] Functional insights into ankyrin-B function have come from studies employing ankyrin-B chimeric proteins. One study showed that the death/C-terminal domain of ankyrin-B determines both the subcellular localization as well as activity in restoring normal inositol trisphosphate receptor and ryanodine receptor localization and cardiomyocyte contractility.[8] Further studies have shown that the beta-hairpin loops within the ankyrin repeat domain of ankyrin-B are required for the interaction with the inositol trisphosphate receptor, and a reduction of ankyrin-B in neonatal cardiomyocytes reduces the half-life of the inositol trisphosphate receptor by 3-fold and destabilizes its proper localization; all of ...
Keratin, type II cuticular Hb1 is a protein that in humans is encoded by the KRT81 gene.[5][6][7] The protein encoded by this gene is a member of the keratin gene family. As a type II hair keratin, it is a basic protein which heterodimerizes with type I keratins to form hair and nails. The type II hair keratins are clustered in a region of chromosome 12q13 and are grouped into two distinct subfamilies based on structure similarity. One subfamily, consisting of KRTHB1, KRTHB3, and KRTHB6, is highly related. The other less-related subfamily includes KRTHB2, KRTHB4, and KRTHB5. All hair keratins are expressed in the hair follicle; this hair keratin, as well as KRTHB3 and KRTHB6, is found primarily in the hair cortex. Mutations in this gene and KRTHB6 have been observed in patients with a rare dominant hair disease, monilethrix.[7] ...
The cytokeratins are encoded by a family encompassing 30 genes. Among them, 20 are epithelial genes and the remaining 10 are specific for trichocytes. All cytokeratin chains are composed of a central α-helix-rich domain (with a 50-90% sequence identity among cytokeratins of the same type and around 30% between cytokeratins of different type) with non-α-helical N- and C-terminal domains. The α-helical domain has 310-150 amino acids and comprises four segments in which a seven-residue pattern repeats. Into this repeated pattern, the first and fourth residues are hydrophobic and the charged residues show alternate positive and negative polarity, resulting in the polar residues being located on one side of the helix. This central domain of the chain provides the molecular alignment in the keratin structure and makes the chains form coiled dimers in solution. The end-domain sequences of type I and II cytokeratin chains contain in both sides of the rod domain the subdomains V1 and V2, which have ...
Actin acts as a track for myosin motor motility[edit]. Myosin motors are intracellular ATP-dependent enzymes that bind to and ... Various classes of myosin motors have very different behaviors, including exerting tension in the cell and transporting cargo ... In inducing cell motility, one end of the actin filament elongates while the other end contracts, presumably by myosin II ... This polarity has been determined by the pattern created by the binding of myosin S1 fragments: they themselves are subunits of ...
... was first described in 1976,[16] first purified in 1977,[17] the gene was cloned in 1989,[6] and the first knockout mouse was created in 1996.[18] The function of desmin has been deduced through studies in knockout mice. Desmin is one of the earliest protein markers for muscle tissue in embryogenesis as it is detected in the somites.[12] Although it is present early in the development of muscle cells, it is only expressed at low levels, and increases as the cell nears terminal differentiation. A similar protein, vimentin, is present in higher amounts during embryogenesis while desmin is present in higher amounts after differentiation. This suggests that there may be some interaction between the two in determining muscle cell differentiation. However desmin knockout mice develop normally and only experience defects later in life.[13] Since desmin is expressed at a low level during differentiation another protein may be able to compensate for desmin's function early in development but not ...
Through alternative splicing of the fetal exon and other alternative exons in the N-terminal variable region, the expression of fsTnT during mammalian and avian development undergoes a high molecular to low molecular weight isoform switch in both fast and slow fiber dominant skeletal muscles.[20] The inclusion of more N-terminal exons increases the negative charge that tunes the overall molecular conformation of fsTnT and alters interaction with TnI, TnC and tropomyosin.[21][22][23] The alternative splicing-based addition of N-terminal negative charge in fsTnT also contributes to the tolerance to acidosis.[24] Alternative splicing of the two C-terminal mutually exclusive exons 16 and 17 appears also regulated during development.[14] Exon 17 with a sequence more similar to the counterpart segment in ssTnT and cTnT is predominantly expressed in embryonic and neonatal fsTnT.[14][25] Exon 16 of fsTnT was only found in adult skeletal muscles. Exons 16 and 17 both encode a 14 amino acids peptide ...
Actin, desmin, myosin, and tropomyosin". The American Journal of Pathology. 142 (1): 221-30. PMC 1886840. PMID 8424456. Tiso N ... myosin ATPase activity, and the cardiac response to stress. A decrease in β-tropomyosin in patients with heart failure was ... troponin C and troponin T-to modulated the actin and myosin interaction. In diastole, the tropomyosin-troponin complex inhibits ...
Surks HK, Riddick N, Ohtani K (2006). "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain ... Surks HK, Richards CT, Mendelsohn ME (2004). "Myosin phosphatase-Rho interacting protein. A new member of the myosin ... Koga Y, Ikebe M (2005). "p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by ... Myosin phosphatase Rho-interacting protein is an enzyme that in humans is encoded by the MPRIP gene. M-RIP has been shown to ...
Surks HK, Richards CT, Mendelsohn ME (2003). "Myosin phosphatase-Rho interacting protein. A new member of the myosin ... The gene encodes a subunit of myosin phosphatase. The encoded protein regulates the catalytic activity of protein phosphatase 1 ...
This phosphorylation results in higher ATPase activity and the assembly of myosin II filaments. "Myosin, light chain 12B, ... Myosin, light chain 12B, regulatory is a protein that in humans is encoded by the MYL12B gene. The gene is also known as MLC-B ... The activity of nonmuscle myosin II is regulated by phosphorylation of a regulatory light chain, such as MYL12B. ...
Myosin-XVIIIa is a protein that in humans is encoded by the MYO18A gene. GRCh38: Ensembl release 89: ENSG00000196535 - Ensembl ... "Entrez Gene: MYO18A myosin XVIIIA". Chroneos ZC, Abdolrasulnia R, Whitsett JA, et al. (1996). "Purification of a cell-surface ... 2005). "Identification of the surfactant protein A receptor 210 as the unconventional myosin 18A". J. Biol. Chem. 280 (41): ... "Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A)". J Biochem. ...
Most frequent side effects are nausea, orthostatic hypotension, headaches, and vomiting through stimulation of the brainstem vomiting centre.[9] Vasospasms with serious consequences such as myocardial infarction and stroke that have been reported in connection with the puerperium, appear to be extremely rare events.[10] Peripheral vasospasm (of the fingers or toes) can cause Raynaud's Phenomenon. Bromocriptine use has been anecdotally associated with causing or worsening psychotic symptoms (its mechanism is in opposition of most antipsychotics, whose mechanisms generally block dopamine).[11] Pulmonary fibrosis has been reported when bromocriptine was used in high doses for the treatment of Parkinson's disease.[12] Use to suppress milk production after childbirth was reviewed in 2014 and it was concluded that in this context a causal association with serious cardiovascular, neurological or psychiatric events could not be excluded with an overall incidence rate estimated to range between 0.005% ...
InChI=1S/C25H29N3O2/c1-27-14-18(13-26-25(29)30-16-17-7-4-3-5-8-17)11-21-20-9-6-10-22-24(20)19(12-23(21)27)15-28(22)2/h3-10,15,18,21,23H,11-14,16H2,1-2H3,(H,26,29)/t18-,21+,23+/m0/s1 ...
Myosin XII[edit]. Myosin XIII[edit]. Myosin XIV[edit]. This myosin group has been found in the Apicomplexa phylum.[40] The ... Myosin X[edit]. Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is ... Myosin XVI[edit]. Myosin XVII[edit]. Myosin XVIII[edit]. MYO18A A gene on chromosome 17q11.2 that encodes actin-based motor ... Myosin III[edit]. Myosin III is a poorly understood member of the myosin family. It has been studied in vivo in the eyes of ...
A myosin light chain is a light chain (small polypeptide subunit) of myosin. Myosin light chains were discovered by Chinese ... Myosin light-chain kinase Myosin-light-chain phosphatase Myosin+Light+Chains at the US National Library of Medicine Medical ... Structurally, myosin light chains belong to the EF-hand family, a large family of Ca2+- binding proteins. MLCs contain two Ca2+ ... Myosin light chains (MLCs) can be broadly classified into two groups: Essential or alkali MLC (MLC1 or ELC), Regulatory MLC ( ...
Class V myosins.. Reck-Peterson SL1, Provance DW Jr, Mooseker MS, Mercer JA. ...
myosin (countable and uncountable, plural myosins) *(biochemistry) Any of a large family of motor proteins found in eukaryotic ... Retrieved from "https://en.wiktionary.org/w/index.php?title=myosin&oldid=60980377" ...
Because myosin light chain has no inherent phosphate cleaving property over active PKC prevents the dephosphorylation of myosin ... Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. This myosin binding domain ... Within the cells, MYLK provides an inward pulling force, phosphorylating myosin light chain causing a contraction of the myosin ... Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a ...
In muscle cells myosin is arranged in long filaments called thick filaments that lie parallel to the microfilaments of actin [2 ... myosin (mī´əsĬn), one of the two major protein [1] constituents responsible for contraction of muscle. ... The type of myosin molecule found in muscle fibres consists of a tail, by which it aggregates with other myosin molecules to ... myosin The predominant protein of the myofibrils of muscle cells. It has an unusual shape for a protein, having a globular head ...
The number of known unconventional myosins is increasing rapidly and in the past year alone two new classes have been ... The unconventional myosins form a large and diverse group of molecular motors. ... The unconventional myosins form a large and diverse group of molecular motors. The number of known unconventional myosins is ... Unconventional myosins Curr Opin Cell Biol. 1992 Feb;4(1):27-35. doi: 10.1016/0955-0674(92)90055-h. ...
Myosins: matching functions with motors.. Baker JP1, Titus MA.. Author information. 1. Department of Cell Biology, Duke ... It is an exciting time to be studying myosins and their roles in the function of cells and organisms. Past efforts aimed at ... The following article reviews the inroads made into the functions of myosins in these processes over the past several years. ...
... belongs to the group of class I myosins, which are monomeric, nonprocessive, slow-rate, and low-duty ratio molecular motors... ... MMIb; MMI-beta; Myo1C isoform B; myr2; NM1; NMI Nuclear myosin I (NM1) ... the first single-headed myosin isolated from mammals, also known as mammalian myosin I, or myosin 1β. However, with the ... Nuclear myosin I (NM1) belongs to the group of class I myosins, which are monomeric, nonprocessive, slow-rate, and low-duty ...
Myosin storage myopathy is a condition that causes muscle weakness (myopathy) that does not worsen or worsens very slowly over ... Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms. Proc Natl Acad Sci U S A. 2009 Apr 14; ... Mutations in the MYH7 gene cause myosin storage myopathy. The MYH7 gene provides instructions for making a protein known as the ... Cardiac β-myosin heavy chain is the major component of the thick filament in muscle cell structures called sarcomeres. . ...
... www.jbc.org/content/291/43/22373.full Single spots binding to actin stress fibres are myosin-6 mini-filame... ... Myosin-2b-GFP molecules in HeLa cell @37°C. http:// ...
... although there is general agreement in the naming of myosins I in vertebrates (Gillespie et al. 2001). The names used in ... The nomenclature of myosins I is confusing, although there is general agreement in the naming of myosins I in vertebrates ( ... Myosin 1 is the largest of ∼35 different classes of proteins that comprise the myosin superfamily, a collection of actin- ... Transient kinetic analysis of the 130-kDa myosin I (myr 1 gene product) from rat liver: a myosin I designed for maintenance of ...
Myosin definition is - a fibrous globulin of muscle that can split ATP and that reacts with actin in muscle contraction to form ... Comments on myosin. What made you want to look up myosin? Please tell us where you read or heard it (including the quote, if ... Post the Definition of myosin to Facebook Share the Definition of myosin on Twitter ... Examples of myosin in a Sentence. Recent Examples on the Web. Hundreds or thousands of amino acids are linked together to form ...
myosin synonyms, myosin pronunciation, myosin translation, English dictionary definition of myosin. n. Any of a class of ... myosin. Also found in: Thesaurus, Medical, Acronyms, Encyclopedia, Wikipedia.. Related to myosin: Myosin light chain kinase ... Phosphorylation by ROCK inactivates a myosin phosphatase, retaining myosin II in the phosphorylated or active state [34, 35].. ... Myosin - definition of myosin by The Free Dictionary https://www.thefreedictionary.com/myosin ...
... x011 at Lehigh.EDU x011 at Lehigh.EDU Fri Mar 24 09:03:28 EST 1995 *Previous message: ... The data curve supports this with a ossilation of 50/50 hook up of the myosin/kinesin system to the microtubules. It is ... Gilbert et al reports that myosin and kinesin are binary switching in the microtubules. These dimer actions I naturally see as ...
Myosin XIIEdit. Myosin XIIIEdit. Myosin XIVEdit. This myosin group has been found in the Apicomplexa phylum.[37] The myosins ... Myosin XEdit. Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is ... "Myosin". Merriam-Webster Dictionary.. *^ "myosin - definition of myosin in English from the Oxford dictionary". ... Myosin IIIEdit. Myosin III is a poorly understood member of the myosin family. It has been studied in vivo in the eyes of ...
Class III myosin, motor domain (IPR036083). Short name: MYSc_Myo3 Domain relationships *Myosin head, motor domain (IPR001609) * ... Myosin III is an actin-based motor protein with protein kinase activity [PMID: 12672820]. It has been shown to play a role in ... Determination of human myosin III as a motor protein having a protein kinase activity.. J. Biol. Chem. 278 21352-60 2003 ... Class III myosins shape the auditory hair bundles by limiting microvilli and stereocilia growth.. J. Cell Biol. 212 231-44 2016 ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Discovery of myosin genes by physical mapping in Dictyostelium. M A Titus, A Kuspa, and W F Loomis ... The previously identified myosin loci (mchA, myoA-E) were detected by hybridization to the probes, as well as an additional ... The diversity of the myosin family in a single organism, Dictyostelium discoideum, has been investigated by a strategy devised ... genome was probed at low stringency with conserved regions of the myosin motor domain to identify all possible myosin loci. ...
Myosin Filament - What happens to me during a contraction of the muscle? by carrie mcclure , This newsletter was created with ... What is Myosin? And what do i do during a contraction? First of all myosin is a chemical that is in the muscles and it works ... The myosin is always grabbing at the actin with the myosin heads, and they to try and attach to it but it cant unless we have ... Myosin Filament What happens to me during a contraction of the muscle? ...
Dynamics of actin/myosin coalescence. (A) Trajectories of myosin filaments moving on an actin network (1∶200 myosin∶actin; 3 ... We used myosin filaments with an average length of 0.69 μm (Fig. 1E) or approximately 100 myosin motors (39). This size is ... Occasionally, two neighboring myosin filaments came together and fused into a small myosin focus (Fig. 2B and Movie S4). Upon ... Initially, myosin foci formation did not drastically reshape the actin network (sketched in Fig. 1A iv). However, once myosin ...
Recently, it has been shown that a gene encoding an unconventional myosin, myosin VIIA, underlies the mouse recessive deafness ... Recently, it has been shown that a gene encoding an unconventional myosin, myosin VIIA, underlies the mouse recessive deafness ... Liu, X., Walsh, J., Mburu, P. et al. Mutations in the myosin VIIA gene cause non-syndromic recessive deafness. Nat Genet 16, ... Myosin VIIA gene: Heterogeneity of the mutations responsible for Usher syndrome type IB. Hum. Mol. Genet. 6, 111-116 (1997). ...
Buy our Myosin VIIa peptide. Ab4996 is a blocking peptide and has been validated in BL. Abcam provides free protocols, tips and ... Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their ... In retina, myosin VIIa may play a role in trafficking of ribbon-synaptic vesicle complexes and renewal of the outer ... may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and myosin ...
Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their ... Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. Binds to the membrane receptors SEC4 ...
... Maegen A. Ackermann and Aikaterini Kontrogianni- ... Maegen A. Ackermann and Aikaterini Kontrogianni-Konstantopoulos, "Myosin Binding Protein-C Slow: An Intricate Subfamily of ...
Characterization of myosin-A and myosin-C: two class XIV unconventional myosins from Toxoplasma gondii. Cell Motil. ... Until now, no myosin of class II or V has been identified in Apicomplexa. To assign which myosin could be involved in the cell ... It is noteworthy that for a long time, among the hundreds of myosins known, only the conventional myosins of class II had been ... Toxoplasma gondii myosins B/C. Frédéric Delbac, Astrid Sänger, Eva M. Neuhaus, Rolf Stratmann, James W. Ajioka, Catherine ...
Actin Myosin Protocols. Protocols and information relating to actin and myosin. Protocols » Cytoskeleton Protocols » Actin ... Actin Myosin Protocols Protocol Links. Actin Binding & Bundling Sedimentation Assays Protocol includes: Binding assays for ...
Embryonic myosin heavy-chain mutations cause distal arthrogryposis and developmental myosin myopathy that persists postnatally. ... BACKGROUND: Myosin is a molecular motor and the essential part of the thick filament of striated muscle. The expression of ... CONCLUSIONS: Distal arthrogryposis associated with MYH3 mutations is secondary to myosin myopathy, and postnatal muscle ... Myosin Heavy Chains, genetics, physiology, Prenatal Diagnosis, methods, Protein Isoforms, genetics, physiology ...
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Myosin: Biosynthesis, Classes and Function opens with a discussion on class I myosins, the most varied members of the myosin ... Myosin: Biosynthesis, Classes and Function. David Broadbent (Editor). Series: Cell Biology Research Progress. BISAC: SCI017000 ... Thus, the authors name the 46-48 kDa proteins revealed in a blood serum as a short form of the human unconventional myosin 1c ( ... Home / Shop / Books / Science and Technology / Life Sciences / Biology / Cell Biology / Myosin: Biosynthesis, Classes and ...
  • Structurally, myosin light chains belong to the EF-hand family, a large family of Ca2+- binding proteins. (wikipedia.org)
  • Among them are, for example, MYL6B, MYLIP, MYLK, and MYLK2, Several diseases have been associated with mutations in the genes encoding for myosin light chain proteins. (wikipedia.org)
  • Myosins ( / ˈ m aɪ ə s ɪ n , - oʊ -/ [1] [2] ) are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes . (wikipedia.org)
  • The neck domain can also serve as a binding site for myosin light chains which are distinct proteins that form part of a macromolecular complex and generally have regulatory functions. (wikipedia.org)
  • The nomenclature can therefore be somewhat confusing when attempting to compare the functions of myosin proteins within and between organisms. (wikipedia.org)
  • Similar filament-forming myosin proteins were found in cardiac muscle, smooth muscle, and nonmuscle cells. (wikipedia.org)
  • However, beginning in the 1970s, researchers began to discover new myosin genes in simple eukaryotes [3] encoding proteins that acted as monomers and were therefore entitled Class I myosins. (wikipedia.org)
  • Myosin 1 is the largest of ∼35 different classes of proteins that comprise the myosin superfamily, a collection of actin-associated molecular motor proteins that use the energy from ATP. (springer.com)
  • Myosin I. Proteins Cell Reg. (springer.com)
  • Hundreds or thousands of amino acids are linked together to form proteins such as insulin, collagen, dystrophin, myosin , and the thousands of others needed for life. (merriam-webster.com)
  • Sharon Begley, STAT , "Genome 'writers' set their first goal: recoding human cells to resist viruses," 1 May 2018 That means making sure the cells have myosin and actin - two proteins that are key to forming the cellular cytoskeleton, and to building muscle filaments. (merriam-webster.com)
  • In preclinical studies, MYK-224 was shown to attenuate hyperactive myosin proteins containing known pathogenic HCM mutations. (thefreedictionary.com)
  • According to our previous studies [5,12], the major factors leading to PSE-like meat having poor protein functionalities are concluded as protein conformation, characteristic of salt soluble proteins, myosin and actin denaturation during meat processing, which also depend on pH and ionic strength conditions. (thefreedictionary.com)
  • To assess the mechanisms leading to protein aggregation in myosin storage myopathy and to evaluate the impact of these mutations on myosin assembly and muscle function, we expressed mutated myosin proteins in cultured human muscle cells and in the nematode Caenorhabditis elegans. (gu.se)
  • Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. (rcsb.org)
  • Maegen A. Ackermann and Aikaterini Kontrogianni-Konstantopoulos, "Myosin Binding Protein-C Slow: An Intricate Subfamily of Proteins," Journal of Biomedicine and Biotechnology , vol. 2010, Article ID 652065, 10 pages, 2010. (hindawi.com)
  • Myosin VIIa is a member of the myosin superfamily of actin-based motor proteins. (abcam.com)
  • This raft protein is lost from the apical surface when a fragment of either myosin-1A or SI interferes with the link between the two full-length proteins. (rupress.org)
  • Tyska is now determining whether the myosin-1A-SI link is regulated by signaling proteins or bacterial toxins. (rupress.org)
  • However, dendritic proteins enable the vesicles transporting them to bind to a second motor, known as myosin , that literally walks them back into the dendrite. (wordnik.com)
  • Until recently, scientists thought RGS proteins, which are found only in small quantities in the heart -- a thousand times less than other, more common proteins, such as myosin and metabolic proteins -- played no key role in heart function. (wordnik.com)
  • Myosins are a large super-family of motor proteins that move along actin filaments, while hydrolyzing ATP to forms of mechanical energy that can be used for a variety of functions such as muscle movement and contraction. (wikibooks.org)
  • Myosin has groups of protein that divide the motor proteins. (wikibooks.org)
  • Among the proteins whose genes have been linked to deafness are several types of myosin. (wikibooks.org)
  • We offer Myosin heavy chain 15 Peptides and Myosin heavy chain 15 Proteins for use in common research applications: Blocking/Neutralizing, Control. (novusbio.com)
  • Our Myosin heavy chain 15 Peptides and Myosin heavy chain 15 Proteins can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Myosin heavy chain 15 Peptides and Proteins. (novusbio.com)
  • A novel protein post-translational modification, citrullination was shown previously in a number of key myofilament proteins, tropomyosin (R 133, R 238), actin (R 39) and myosin heavy chain (R 1176, 1303, 1434) in HF patient (values for total spectra counts for citrullinated proteins in control, ISHD and IDCM: 1.8 ±1.3, 3.2±2.7 and 2.3±1.9, respectively). (ahajournals.org)
  • Citrullination of specific myofilament proteins in HF can have dramatic effect on modulating actin filament integrity and myosin function and tropomyosin action on myofilament regulation. (ahajournals.org)
  • Many myosin light chains that bind calcium are considered "calmodulin-like" proteins. (harvard.edu)
  • Myofibrils consist of contractile proteins called SARCOMERES Name the two types and what they're composed of: THICK FILAMENTS composed of MYOSIN THIN FILAMENTS composed of ACTIN 8. (majortests.com)
  • At first, I purified actomyosin preparations, which were thought to be composed of actin, myosin, and regulatory proteins. (thefreelibrary.com)
  • A gene on chromosome 19p13.1 that encodes a protein belonging to the myosin family of actin-based molecular motor heavy chain proteins, which binds calmodulin, which serves as a light chain. (thefreedictionary.com)
  • Although several myofilament proteins are modified by protein phosphorylation, the 18-kDa myosin light chain 2 (MLC2) has special significance. (ahajournals.org)
  • In general, myosins are protein complexes consisting of one or more myosin heavy chains, associated light chains and other proteins. (rockland-inc.com)
  • The gene for myosin light chain kinase encodes three proteins: MLCK210, MLCK108, and telokin/kinase-related protein (KRP). (springer.com)
  • Organization of the genetic locus for chicken myosin light chain kinase is complex: multiple proteins are encoded and exhibit differential expression and localization. (springer.com)
  • The morphological diversity and distinct dynamics of mammalian actin structures are established by coordinating the targeting and activation of actin filament nucleators, elongators and associated myosin motor proteins. (biologists.org)
  • After a 4-year postdoc in the lab of Prof. Jerry Hyams studying myosin actin associated motor proteins he was awarded a BBSRC David Phillips Fellowship and moved to the University of Kent to continue research on these conserved molecular motors. (babraham.ac.uk)
  • Myosins are actin-based motor proteins involved in many cellular movements. (ncbs.res.in)
  • The identification of large classes of myosins in Oomycetes, Cellular slime molds, Choanoflagellates, Pelagophytes, Eustigmatophyceae, Fonticula, Eucoccidiorida, and Apicomplexans with novel myosin motif variants that are conserved and thus presumably functional extends our knowledge of this important family of motor proteins. (ncbs.res.in)
  • The activity of the myosin light chain phosphatase in dephosphorylation of myosin light chains was first demonstrated using proteins isolated from the turkey gizzard (Pato and Kerc 1985). (reactome.org)
  • Nevertheless, the association of MLCs with the neck region of MHCs is necessary for the assembly of the macromolecular complexes that result in the functional motor protein, myosin. (wikipedia.org)
  • Myosin light-chain kinase also known as MYLK or MLCK is a serine/threonine-specific protein kinase that phosphorylates a specific myosin light chain, namely, the regulatory light chain of myosin II. (wikipedia.org)
  • After the influx of calcium ions and the binding to calmodulin, pp60 SRC (a protein kinase)causes a conformational change in MYLK, activating it and resulting in an increase in phosphorylation of myosin light chain at serine residue 19. (wikipedia.org)
  • Rho kinase also modulates the activity of MYLK by downregulating the activity of MYLK's counterpart protein: Myosin Light Chain Phosphatase (MYLP). (wikipedia.org)
  • In addition to downregulation of MYLK, ROCK indirectly strengthens actin/myosin contraction through inhibiting Cofilin, a protein which depolymerizes actin stress fibers. (wikipedia.org)
  • Another source of smooth muscle disorders like ischemia-reperfusion, hypertension, and coronary artery disease arise when mutations to protein kinase C (PKC) result in excessive inhibition of MYLP, which counteracts the activity of MYLK by dephosphorylating myosin light chain. (wikipedia.org)
  • Because myosin light chain has no inherent phosphate cleaving property over active PKC prevents the dephosphorylation of myosin light protein leaving it in the activated conformation, causing an increase in smooth muscle contraction. (wikipedia.org)
  • This protein makes up part of the sarcomere and forms macromolecular filaments composed of multiple myosin subunits. (wikipedia.org)
  • myosin A contractile protein that interacts with actin to bring about contraction of muscle or cell movement. (encyclopedia.com)
  • myosin The predominant protein of the myofibrils of muscle cells. (encyclopedia.com)
  • The antibody was staining a 120 kDa nuclear protein with ATPase activity, and the protein was ATP-, actin-, and calmodulin- binding, which are the typical features of unconventional myosins. (springer.com)
  • At that time, there were no myosins known to be present in the cell nucleus, hence the discovered protein was called nuclear myosin I (Pestic-Dragovich et al. (springer.com)
  • 2000 ). The mass spectrometric analysis of the NM1 showed a high homology to the Myosin 1c (Myo1c) protein, the first single-headed myosin isolated from mammals, also known as mammalian myosin I, or myosin 1β. (springer.com)
  • This condition is characterized by the formation of protein clumps, which contain a protein called myosin, within certain muscle fibers. (medlineplus.gov)
  • The MYH7 gene provides instructions for making a protein known as the cardiac beta (β)-myosin heavy chain. (medlineplus.gov)
  • Mutations in the MYH7 gene lead to the production of an altered cardiac β-myosin heavy chain protein, which is thought to be less able to form thick filaments. (medlineplus.gov)
  • The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. (springer.com)
  • In the first phase of ontogenesis, the level of myosin in piglets intact platelets was also low, accounting for 10.9 [+ or -] 0.09% of the total protein content in the platelet, reaching 18.3[+ or -]0.09% of the total protein content of the platelet by 12 months. (thefreedictionary.com)
  • More than 80 MYO7A mutations have been identified and are known to inherit in a recessive manner.11 This gene encode protein, the myosin VIIA, expressed in inner ear, retina, testis and lungs. (thefreedictionary.com)
  • In meat samples, the main protein bands identified in the range of molecular weights from 250 to 10kDa were myosin heavy chain (MHC), [alpha]-actinin ([alpha]-act), desmin, actin (ACT), troponin T (TnT), tropomyosin (TPM), myosin light chains 1 (MLC1), troponin C (TnC), and myosin light chains 2 (MLC2). (thefreedictionary.com)
  • Myosin III is an actin-based motor protein with protein kinase activity [ PMID: 12672820 ]. (ebi.ac.uk)
  • Class III myosins are characterized by the presence of an N-terminal protein kinase domain before their motor head domain. (ebi.ac.uk)
  • Determination of human myosin III as a motor protein having a protein kinase activity. (ebi.ac.uk)
  • Myosin storage myopathy is a protein aggregate myopathy associated with the characteristic subsarcolemmal accumulation of myosin heavy chain in muscle fibers. (gu.se)
  • While L1793P mutant myosin protein efficiently incorporated into the sarcomeric thick filaments, R1845W and H1901L mutants were prone to formation of myosin aggregates without assembly into striated sarcomeric thick filaments in cultured muscle cells. (gu.se)
  • By Western blot, this antibody detects an ~220 kDa protein representing myosin VIIa from mouse testes preparations. (abcam.com)
  • Structural features of myosin VIIa protein include an ATP binding N-terminal motor domain, a central region which possess five light-chain binding (IQ) motifs, and a C-terminal domain with three myosin tail homology (MyTH4) and talin-like homology regions. (abcam.com)
  • Here we report the identification in C. elegans of nonmuscle myosin II heavy chain (designated NMY-2) by means of its interaction with the PAR-1 protein, a putative Ser/Thr protein kinase. (nih.gov)
  • The motor protein myosin , for example, is involved in the the contraction of muscle fibers in animals. (wordnik.com)
  • Tail domains have various functions in different myosin classes, including dimerization and other protein-protein interactions. (wikibooks.org)
  • Myosin is a common protein found in the muscles which are responsible for making the muscle contract and relax. (wikibooks.org)
  • Maegen A. Ackermann and Aikaterini Kontrogianni-Konstantopoulos, "Myosin Binding Protein-C: A Regulator of Actomyosin Interaction in Striated Muscle," Journal of Biomedicine and Biotechnology , vol. 2011, Article ID 636403, 9 pages, 2011. (hindawi.com)
  • The rabbit monoclonal antibody is produced by immunizing rabbits with a synthetic peptide corresponding to residues near the carboxy terminus of human myosin light chain 2 protein. (cellsignal.com)
  • Myosin is a hexameric protein that consists of 2 heavy chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory light chain subunits (MLC-2). (pathwaycommons.org)
  • Each Myosin heavy chain 15 Peptide and Myosin heavy chain 15 Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Myosin is the major contractile protein in muscle. (diva-portal.org)
  • Myosin binding protein C (MyBP-C), plays a physiological role in regulating contraction. (diva-portal.org)
  • Name the two types and what theyre composed of ____ thin filament ___________ composed of ______ The protein Actin _____________ _______ thick filament ________ composed of _____ The protein myosin. (majortests.com)
  • Myosin light chain 3, or MYL3 for short, consists of a 195 amino acid isoform that is 22 kDa, and is involved in the regulation of Myosin, which is a protein that conducts ATP hydrolysis. (novusbio.com)
  • Physarum was a good model organism for protein chemistry, because it can be cultured in the lab in large quantities, (2) and because the procedures for purifying actin (3) and myosin (4) were similar to those for skeletal muscle. (thefreelibrary.com)
  • This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an internal region of human Myosin 1G protein. (rockland-inc.com)
  • By western blot a band approximately 100 kDa in size corresponding to Myosin 1G protein is expected in the appropriate cell lysate or extract. (rockland-inc.com)
  • This affinity-purified antibody is directed against human Myosin 1G protein. (rockland-inc.com)
  • The first protein discovered was MLCK108 (Mr = 110-140 kDa) as a major cytoplasmic component of smooth muscle and responsible for smooth muscle contractility through the phosphorylation of the regulatory light chain of myosin (Lukas et al. (springer.com)
  • A kinase-related protein stabilizes unphosphorylated smooth muscle myosin minifilaments in the presence of ATP. (springer.com)
  • Myosin protein (orange structure) is used to transfer energy in cells. (sciencephoto.com)
  • Actin and myosin are protein filaments that functions in the presence of calcium ions.actin and myosin are the striations in skeletal muscles. (differencebetween.net)
  • This myosin molecule is a very big protein composed of two similar chains that are heavy and two pairs of chains that are light. (differencebetween.net)
  • Effects of C-protein on synthetic myosin filament structure. (semanticscholar.org)
  • HCM can be caused by disparate mutated genes in myosin - a fibrous protein involved in the motion of muscle cells and others - and myosin-related molecules, so giving the same treatment to a heterogeneous group of patients can lead to discrepancies in the treatment's effectiveness. (stanforddaily.com)
  • Determination of the critical residues responsible for cardiac myosin binding protein C's interactions. (biomedsearch.com)
  • Despite early demonstrations of myosin binding protein C's (MyBP-C) interaction with actin, different investigators have reached different conclusions regarding the relevant and necessary domains mediating this binding. (biomedsearch.com)
  • Tonic protein kinase A activity maintains inactive beta2 integrins in unstimulated neutrophils by reducing myosin light-chain phosphorylation: role of myosin light-chain kinase and Rho kinase. (thefreedictionary.com)
  • Better understood is the case of the melanosome where Rab27a recruits a specific effector called melanophilin, which in turn binds myosin Va. The presence of a linker protein between a Rab and a myosin may represent a general mechanism. (ovid.com)
  • MYBPC1 encodes a member of the myosin-binding protein C family. (antikoerper-online.de)
  • Zusätzlich bieten wir Ihnen Myosin Binding Protein C, Slow Type Proteine (5) und Myosin Binding Protein C, Slow Type Kits (4) und viele weitere Produktgruppen zu diesem Protein an. (antikoerper-online.de)
  • Ackermann, Kontrogianni-Konstantopoulos: Myosin binding protein-C slow is a novel substrate for protein kinase A (PKA) and C (PKC) in skeletal muscle. (antikoerper-online.de)
  • Myosin regulatory light chain 5 (MYL5) is a hexameric ATPase cellular motor protein. (prospecbio.com)
  • Myosin light chain kinase (MLCK) inhibitors are one of the few peptides that can cross the plasma membrane relatively quickly. (wikipedia.org)
  • Myosin light-chain kinase Myosin-light-chain phosphatase Myosin+Light+Chains at the US National Library of Medicine Medical Subject Headings (MeSH) Zhang Y (June 2010). (wikipedia.org)
  • This myosin binding domain is located at the C-Terminus end of the kinase. (wikipedia.org)
  • Glycogen synthase kinase (GSK) 3beta phosphorylates and protects nuclear myosin 1c from proteasome-mediated degradation to activate rDNA transcription in early G1 cells. (springer.com)
  • The level of myosin II phosphorylation is determined by activities of myosin light chain kinase and myosin phosphatase (MP). (biomedsearch.com)
  • Your search returned 5 myosin, light polypeptide kinase 2, skeletal muscle Biomolecules across 4 suppliers. (biocompare.com)
  • Myosin Light Chain Kinase Inhibitors " has 4 results in Products. (rndsystems.com)
  • MicroRNA regulation of nonmuscle myosin light chain kinase expression in human lung endothelium. (springer.com)
  • Basu S, Proweller A. Autoregulatory control of smooth muscle myosin light chain kinase promoter by notch signaling. (springer.com)
  • Cunningham KE, Turner JR. Myosin light chain kinase: pulling the strings of epithelial tight junction function. (springer.com)
  • The long myosin light chain kinase is differentially phosphorylated during interphase and mitosis. (springer.com)
  • Herring BP, El-Mounayri O, Gallagher PJ, Yin F, Zhou J. Regulation of myosin light chain kinase and telokin expression in smooth muscle tissues. (springer.com)
  • Myosin light chain kinase (210 kDa) is a potential cytoskeleton integrator through its unique N-terminal domain. (springer.com)
  • Sp1-mediated nonmuscle myosin light chain kinase expression and enhanced activity in vascular endothelial growth factor-induced vascular permeability. (springer.com)
  • Myosin light chain kinase (MLCK) induces contraction of the perijunctional apical actomyosin ring in response to phosphorylation of the myosin light chain. (frontiersin.org)
  • Role of myosin light chain kinase (MLCK) in selected diseases. (frontiersin.org)
  • Contractile activity in the smooth muscle is regulated by the calcium/calmodulin-dependent phosphorylation of Myosin light chain by Myosin light chain kinase. (prospecbio.com)
  • It is thought that MLCK phosphorylates endothelial myosin, leading to cell contraction. (wikipedia.org)
  • The phosphorylation of MLC will enable the myosin crossbridge to bind to the actin filament and allow contraction to begin (through the crossbridge cycle). (wikipedia.org)
  • Reducing intracellular calcium concentration inactivates MLCK but does not stop smooth muscle contraction since the myosin light chain has been physically modified through phosphorylation(and not via ATPase activity). (wikipedia.org)
  • Dephosphorylation of the myosin light chain (and subsequent termination of muscle contraction) occurs through activity of a second enzyme known as myosin light-chain phosphatase (MLCP). (wikipedia.org)
  • Within the cells, MYLK provides an inward pulling force, phosphorylating myosin light chain causing a contraction of the myosin/actin stress fiber complex. (wikipedia.org)
  • This also makes what is called tropomyosin, which is the combination of the myosin and troponin come together during the muscle contraction. (smore.com)
  • Phosphorylation of myosin II plays an important role in many cell functions, including smooth muscle contraction. (biomedsearch.com)
  • As the structural and thermodynamic data about ATP mounted, combined with the enzymatic information and the discovery of myosin , Meyerhof was finally in a position to formally propose that the release of energy in ATP hydrolysis was the primary event leading to muscle contraction and that lactic acid and creatine phosphate were only indirectly involved through their role of maintaining the ATP cycle. (wordnik.com)
  • This relative movement between myosin and actin is what results in muscle contraction. (wikibooks.org)
  • Myosin II is essential for muscle contraction and cytokinesis but other members of the myosin superfamily play roles in phagocytosis, cortical cell tension, signal transduction, endocytosis, exocytosis, and intracellular vesicle transport. (esrf.eu)
  • Myosin light chain 3 has been linked to the RhoA pathway, as well as PKA signaling, growth cone motility, cell adhesion, cardiac muscle contraction, and cytoskeleton remodeling. (novusbio.com)
  • Biophysical and biochemical studies have found that OM increases calcium (Ca2+) sensitivity of contraction by prolonging the myosin working stroke and increasing the actin-myosin cross-bridge duty ratio. (unboundmedicine.com)
  • Muscle contraction where actin and myosin functions, are best explained under the sliding filament theory. (differencebetween.net)
  • ATP is needed by myosin to crawl along to actin to create mechanical energy or what we call earlier as muscle contraction. (differencebetween.net)
  • 1.Actin and myosin are found in muscles and function for muscle contraction. (differencebetween.net)
  • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. (semanticscholar.org)
  • An unconventional myosin in Drosophila reverses the default handedness in visceral organs. (springer.com)
  • Both calmodulin and the unconventional myosin Myr4 regulate membrane trafficking along the recycling pathway of MDCK cells. (springer.com)
  • Recently, it has been shown that a gene encoding an unconventional myosin, myosin VIIA, underlies the mouse recessive deafness mutation, shaker-1 (ref. 5) as well as Usher syndrome type 1b 6 . (nature.com)
  • Based on kinetic evidence that an unconventional myosin, class V myosin, populates a unique state in the absence of nucleotide and actin, we hypothesised that its high resolution structure could for the first time reveal features of a strong actin-binding, force generating state. (esrf.eu)
  • Myosin 1G is an unconventional myosin that is restricted to hematopoietic cells. (rockland-inc.com)
  • Cardiac β-myosin heavy chain is the major component of the thick filament in muscle cell structures called sarcomeres . (medlineplus.gov)
  • Because of lacking cardio specificity, we abandoned the myosin light chain work and in 1989 finally published our work on the assay development for cardiac troponin T (cTnT) jointly with Boehringer Mannheim (3). (thefreedictionary.com)
  • Mutations located in the distal end of the tail of slow/beta-cardiac myosin heavy chain are associated with myosin storage myopathy. (gu.se)
  • Cytokinetics, Incorporated (Nasdaq: CYTK) announced today the publication of preclinical research in the March 18, 2011 issue of the journal Science regarding the activation of cardiac myosin by an investigational drug candidate, omecamtiv mecarbil, and the potential therapeutic role that this novel mechanism may play for patients with systolic heart failure. (redorbit.com)
  • The publication titled, "Cardiac Myosin Activation: A Potential Therapeutic Approach for Systolic Heart Failure," discusses the potential clinical role for therapies that directly activate cardiac myosin in the treatment of systolic heart failure. (redorbit.com)
  • Omecamtiv mecarbil, a small-molecule, direct activator of cardiac myosin, was developed to address these limitations. (redorbit.com)
  • The authors concluded that cardiac myosin activation may provide a new therapeutic approach for patients with systolic heart failure. (redorbit.com)
  • Omecamtiv mecarbil, a novel cardiac muscle myosin activator, has been the subject of a clinical trials program comprised of multiple Phase I and Phase IIa trials conducted under Cytokinetics' sponsorship. (redorbit.com)
  • The antibodies do not cross-react with the cardiac isoform of Myosin Light Chain 2. (cellsignal.com)
  • CK-274 is a novel cardiac myosin inhibitor, discovered by company scientists, in development for the potential treatment of hypertrophic cardiomyopathy (HCM). (yahoo.com)
  • CK-274 is a novel, oral, small molecule cardiac myosin inhibitor that company scientists discovered independent of its collaborations. (yahoo.com)
  • In preclinical models, CK-274 reduces myocardial contractility by binding directly to cardiac myosin at a distinct and selective allosteric binding site, thereby preventing myosin from entering a force producing state. (yahoo.com)
  • CK-274 reduces the number of active actin-myosin cross bridges during each cardiac cycle and consequently reduces myocardial contractility. (yahoo.com)
  • Omecamtiv mecarbil (OM) is a compound that has been developed to treat systolic heart failure via targeting the cardiac myosin heavy chain to increase myocardial contractility. (unboundmedicine.com)
  • Nuclear myosin 1c facilitates the chromatin modifications required to activate rRNA gene transcription and cell cycle progression. (springer.com)
  • Mutations in the MYH7 gene cause myosin storage myopathy. (medlineplus.gov)
  • Transient kinetic analysis of the 130-kDa myosin I (myr 1 gene product) from rat liver: a myosin I designed for maintenance of tension? (springer.com)
  • The diversity of the myosin family in a single organism, Dictyostelium discoideum, has been investigated by a strategy devised to rapidly identify and clone additional members of a gene family. (pnas.org)
  • In C. elegans, mutant alleles of the myosin heavy chain gene unc-54 corresponding to R1845W, E1883K and H1901L, were as effective as the wild-type myosin gene in rescuing the null mutant worms, indicating that they retain functionality. (gu.se)
  • A type VII myosin encoded by the mouse deafness gene shaker-1. (nature.com)
  • Defective myosin VIIA gene responsible for Usher syndrome type 1B. (nature.com)
  • Liu, X.Z., Newton, V.E., Steel, K.P. & Brown, S.D.M. Identification of a new mutation of the head region of myosin VII gene in Usher syndrome type 1. (nature.com)
  • Defects in the myosin VIIa gene are responsible for hearing impairment in shaker-1 (sh1) mice and causes Usher syndrome IB in humans. (abcam.com)
  • Sequence requirements for myosin gene expression and regulation in Caenorhabditis elegans. (genetics.org)
  • We have used transformation-rescue and lacZ fusion assays to determine sequence requirements for regulated myosin gene expression during development. (genetics.org)
  • To further characterize the myosin gene promoters and to examine the types of enhancer sequences in the genome, we have initiated a screen of C. elegans genomic DNA for fragments capable of enhancing the myo-2 promoter. (genetics.org)
  • We have isolated spontaneous mutations affecting the unc-54 major myosin heavy chain gene of Caenorhabditis elegans (variety Bristol). (genetics.org)
  • Telokin/KRP is an independently expressed nonkinase gene product containing the C-terminus of MLCK, and functions as a myosin-binding and. (springer.com)
  • Myosin XIX gene silencers are available as Myosin XIX CRISPR/Cas9 Knockout plasmids and Myosin XIX Double Nickase Plasmids. (scbt.com)
  • Myosin XIX CRISPR/dCas9 Activation Plasmids and CRISPR Lenti Activation Systems for gene activation are also available. (scbt.com)
  • Armel TZ, Leinwand LA. Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms. (medlineplus.gov)
  • Embryonic myosin heavy-chain mutations cause distal arthrogryposis and developmental myosin myopathy that persists postnatally. (gu.se)
  • CONCLUSIONS: Distal arthrogryposis associated with MYH3 mutations is secondary to myosin myopathy, and postnatal muscle manifestations are variable. (gu.se)
  • Mutations introduced into the ATPase domain of non-muscle myosin-2 (NMY-2, the sole myosin required for early cytokinesis) bind to actin but fail to translocate it in vitro . (biologists.org)
  • The discovery that mutations in myosin and actin genes, together with mutations in the other components of the muscle sarcomere, are responsible for a range of inherited muscle diseases (myopathies) has revolutionized the study of muscle, converting it from a subject of basic science to a relevant subject for clinical study and has been responsible for a great increase of interest in muscle studies. (mdpi.com)
  • Myopathies are linked to mutations in five of the myosin heavy chain genes, three of the myosin light chain genes, and three of the actin genes. (mdpi.com)
  • To address this problem, biochemistry professor James Spudich Ph.D. '68, pediatrics and cardiology professor Daniel Bernstein and cardiovascular medicine associate professor Sean Wu B.S. '92 led a research project focusing on how mutations in myosin - specifically in the heart - lead to the development of HCM. (stanforddaily.com)
  • We are examining this problem at multiple different scales: from the individual molecule to the cell to the tissue, to figure out why these mutations [in myosin] cause life-threatening diseases like hypertrophic cardiomyopathy," Bernstein said. (stanforddaily.com)
  • Equipped with the RM1 grant, the team is transitioning its research from figuring out the mechanism of mutations in myosin to identifying potential methods that would disrupt the pathological mechanism. (stanforddaily.com)
  • The team has also expanded its research on myosin to developing a greater understanding of not only the effects of myosin mutations on heart muscles, but on skeletal muscles and other myosin-related organs in the human body as well. (stanforddaily.com)
  • Presumably this is so the myosins may interact, via their tails, with a large number of different cargoes, while the goal in each case - to move along actin filaments - remains the same and therefore requires the same machinery in the motor. (wikipedia.org)
  • This location is critical for the proper assembly of sarcomeric myosin rod filaments. (gu.se)
  • Here we study how the collective action of myosin motors organizes actin filaments into contractile structures in a simplified model system devoid of biochemical regulation. (pnas.org)
  • Actin-myosin II solutions remain disordered at high levels of ATP ( 12 ⇓ - 14 ) and generate dense condensates that appear internally unstructured if the ATP level is lowered or when the actin filaments are cross-linked ( 15 ⇓ ⇓ - 18 ). (pnas.org)
  • When myosin is activated, the contractile filaments slide apart and the muscle cell relaxes. (wordnik.com)
  • Skeletal muscles contain many muscle fibers and these muscle fibers are actually made up of myofibrils, bundles of thick myosin filaments and thin actin filaments. (wikibooks.org)
  • One region is called the A-bands and only consist of myosin filaments. (wikibooks.org)
  • Actin filaments from the I-bands become very short while myosin filaments from the A-bands do not change in length. (wikibooks.org)
  • The actin filaments are actually sliding towards the H-zone and the A-bands thus creating an overlap of myosin and actin filaments. (wikibooks.org)
  • As this overlap occurs, myosin filaments are binding to the actin filaments, allowing myosin to function as the driving motor of filament sliding. (wikibooks.org)
  • Myosin I appears to cross-link actin filaments to control the tension inside each stereocilium. (wikibooks.org)
  • The ratcheting activity of this myosin motor along the actin filaments may adjust the sensitivity of the hair cells to different sounds. (wikibooks.org)
  • Other types of myosin use their motor activity to redistribute cellular constituents along the length of the actin filaments. (wikibooks.org)
  • Myosins are molecular motors that use cellular ATP to power interactions with actin filaments and create force and directed movement. (esrf.eu)
  • Myosins function as molecular motors and use the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments. (rockland-inc.com)
  • Myosin filaments are responsible for the dark bands or striations, referred as H zone. (differencebetween.net)
  • The head of a myosin which is globular attaches to actin filaments on proper sites. (differencebetween.net)
  • In the sliding theory, actin and myosin filaments slide past each other. (differencebetween.net)
  • When the fibers of the muscles are stimulated by the nervous system, the heads of the myosin attach to the binding sites on the lean filaments, and the sliding starts. (differencebetween.net)
  • X-ray evidence for conformational changes in the myosin filaments of vertebrate striated muscle. (semanticscholar.org)
  • Moreover, quantitative analysis of filament shape change over time revealed that myosin XI generates the force for buckling and straightening of both single actin filaments and actin bundles. (plantphysiol.org)
  • Unlike animal cells, which use microtubules as tracks for long-distance transport, plants use predominantly actin filaments and myosin motors for vesicle trafficking and organelle positioning ( Schuh, 2011 ). (plantphysiol.org)
  • In addition to myosin XI, a functional network of dynamic actin filaments is critical for vesicle trafficking. (plantphysiol.org)
  • Actin filaments or bundles provide the tracks for myosins to processively translocate using the energy of ATP hydrolysis. (plantphysiol.org)
  • We find that contact times increase from isoforms C to B to A, that A-B-heterodimers are surprisingly stable and that myosin 18A should incorporate into mixed filaments with a small stagger. (unboundmedicine.com)
  • Our findings suggest that nonmuscle myosin II minifilaments in the cell are first formed by isoform A and then convert to mixed A-B-filaments, as observed experimentally. (unboundmedicine.com)
  • Skeletal muscle fibre with exposed intracellular actin myosin filaments, scanning electron micrograph (SEM). (sciencephoto.com)
  • The muscle fibre was cut perpendicular to its length to expose the intracellular actin myosin filaments. (sciencephoto.com)
  • Muscle fibres are composed of myofibrils that are composed of actin and myosin filaments. (sciencephoto.com)
  • Regional alterations in the expression of smooth muscle myosin isoforms in response to partial bladder outlet obstruction. (wordnik.com)
  • Up-regulation of transcription of smooth muscle myosin alkali lig. (ingentaconnect.com)
  • The antibodies in the Myosin Light Chain 2 Antibody Sampler Kit detect endogenous levels of total myosin light chain 2 (smooth muscle), myosin light chain 2 when phosphorylated at Ser19 or when dually phosphorylated at Thr18 and Ser19, respectively. (cellsignal.com)
  • A smooth-muscle myosin heavy-chain assay is performed in the first 24 hours. (medscape.com)
  • The smooth muscle myosin heavy-chain assay has greater sensitivity and specificity than transthoracic echocardiography (TTE), CT, and aortography, but it has less sensitivity and specificity than transesophageal echocardiography (TEE), MRI, and helical CT. (medscape.com)
  • A myosin I isoform in the nucleus. (springer.com)
  • Wu HY, Zderic SA, Wein AJ, Chacko S: Decrease in maximal force generation in the neonatal mouse bladder corresponds to shift in myosin heavy chain isoform composition. (wordnik.com)
  • Austin JC, Chacko SK, DiSanto M, Canning DA, Zderic SA: A male murine model of partial bladder outlet obstruction reveals changes in detrusor morphology, contractility and myosin isoform expression. (wordnik.com)
  • 1998) Correlation between contractile strength and myosin heavy chain isoform composition in human skeletal muscle. (acronymfinder.com)
  • Myosin heavy chain isoform expression following reduced neuromuscular activity: Potential regulatory mechanisms. (acronymfinder.com)
  • Myosin light chain 6B, Myosin light chain 1 slow-twitch muscle A isoform, MLC1sa, Smooth muscle and nonmuscle myosin light chain alkali 6B, MYL6B, MLC1SA. (prospecbio.com)
  • Myosin phosphatase: structure, regulation and function. (biomedsearch.com)
  • Confocal immunofluorescent images of HeLa cells, untreated (left) or phosphatase-treated (right), labeled with Phospho-Myosin Light Chain 2 (Ser19) Antibody (green). (cellsignal.com)
  • This targeting domain of MLCP, which is termed myosin binding site (MBS) or myosin phosphatase targeting peptide, binds to myosin or MLC2 and promotes catalytic activity of the 37-kDa domain. (ahajournals.org)
  • Molecular mechanism of telokin-mediated disinhibition of myosin light chain phosphatase and cAMP/cGMP-induced relaxation of gastrointestinal smooth muscle. (springer.com)
  • Myosin light chain phosphatase (MLCP) is an enzyme important to regulation of cell cycle and motility that is shown to be upregulated in aggressive prostate cancer cells and tissue. (frontiersin.org)
  • Our initial aim of this study is to develop a small molecule inhibitor of myosin light chain phosphatase (MLCP) that causes a reduction in cancer cell growth. (frontiersin.org)
  • This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and myosin VIIa, catalog ab3481 . (abcam.com)
  • This antibody detects recombinant mouse myosin VIIa overexpressed in Sf9 insect cell lysate. (abcam.com)
  • Western blot analysis of extracts from HEK293 cells stimulated with ionophore A23187 for the indicated times, using Phospho-Myosin Light Chain 2 (Ser19) Antibody. (cellsignal.com)
  • The Myosin Light Chain 2 Antibody Sampler Kit provides an economical means to detect total, phosphorylated, and dual-phosphorylated myosin light chain 2. (cellsignal.com)
  • Suitable for immunohistochemical applications, Western blotting and immunoprecipitation studies.Anti-Myosin antibody, from rabbit, is used in chemiluminescent western blot (1:200, using whole cell extracts of cultured dog MDCK kidney cells, cultured rat NRK cells, and cultured human Jurkat cells). (alfa.com)
  • Myosin light chains were discovered by Chinese biochemist Cao Tianqin (Tien-chin Tsao) when he was a graduate student at the University of Cambridge in England. (wikipedia.org)
  • Myosin light chains (MLCs) can be broadly classified into two groups: Essential or alkali MLC (MLC1 or ELC), Regulatory MLC (MLC2 or RLC). (wikipedia.org)
  • MLCs are structurally and functionally distinct from myosin heavy chains (MHCs). (wikipedia.org)
  • A myosin complex containing one or more class XVII myosin heavy chains and associated light chains. (semanticscholar.org)
  • Myosin Light Chains" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
  • The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. (harvard.edu)
  • The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. (harvard.edu)
  • This graph shows the total number of publications written about "Myosin Light Chains" by people in Harvard Catalyst Profiles by year, and whether "Myosin Light Chains" was a major or minor topic of these publication. (harvard.edu)
  • Below are the most recent publications written about "Myosin Light Chains" by people in Profiles. (harvard.edu)
  • Myosin is comprised of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains. (prospecbio.com)
  • The reconstitution of myosin with MYL5 or alkali light chain increases filament velocity to intermediate rates, and the re-addition of both classes of light chains fully reinstates the original sliding pace. (prospecbio.com)
  • Most myosin molecules are composed of a head , neck, and tail domain. (wikipedia.org)
  • The tail domain generally mediates interaction with cargo molecules and/or other myosin subunits . (wikipedia.org)
  • Multiple myosin II molecules generate force in skeletal muscle through a power stroke mechanism fuelled by the energy released from ATP hydrolysis. (wikipedia.org)
  • Are class III and class IX myosins motorized signalling molecules? (ebi.ac.uk)
  • Myosins are actin-based motor molecules with ATPase activity. (abcam.com)
  • 2. The myosin head contains binding sites for what two molecules a. (majortests.com)
  • Myosin filament, on the other hand is composed of bundles of myosin molecules. (differencebetween.net)
  • In muscles, two myosin molecules are required. (differencebetween.net)
  • Recent experiments with super-resolution live cell microscopy revealed that nonmuscle myosin II minifilaments are much more dynamic than formerly appreciated, often showing plastic processes such as splitting, concatenation and stacking. (unboundmedicine.com)
  • In apicomplexan parasites, actin-disrupting drugs and the inhibitor of myosin heavy chain ATPase, 2,3-butanedione monoxime, have been shown to interfere with host cell invasion by inhibiting parasite gliding motility. (rupress.org)
  • F-actin-tropomyosin binding, tropomyosin-actin-myosin, actin-myosin and myosin ATPase activity assays, and F-actin stability assays were carried out. (ahajournals.org)
  • Furthermore, citrullination of myosin HMM is not essential for actin affinity, although it modulate ATPase activation (p=0.3). (ahajournals.org)
  • Contrary, the ATPase activity is increase by pretreatment of actin (but not myosin) with PAD2 (p=0.09). (ahajournals.org)
  • Myosin hydrolyses ATP in states that have a weak affinity for actin, and strain is produced when myosin rebinds to the actin filament, which accelerates the release of the ATPase products from the motor. (esrf.eu)
  • Myosins have magnesium-ATPase activity and bind actin. (rockland-inc.com)
  • Heads of myosin contain ATPase that converts ATP to ADP. (differencebetween.net)
  • [3] Following the discovery by Pollard and Korn (1973) of enzymes with myosin-like function in Acanthamoeba castellanii , a global range of divergent myosin genes have been discovered throughout the realm of eukaryotes. (wikipedia.org)
  • The wide variety of myosin genes found throughout the eukaryotic phyla were named according to different schemes as they were discovered. (wikipedia.org)
  • Sequence analysis and physical mapping of these clones confirm that these PCR products are derived from four previously unidentified myosin genes. (pnas.org)
  • Preliminary analysis of these sequences suggests that at least one of the genes (myoJ) encodes a member of a potentially different class of myosins. (pnas.org)
  • Deletion of the genes MYO3 and MYO5 , which encode the yeast type I myosins, almost abolished growth. (sciencemag.org)
  • Discover related pathways, diseases and genes to Myosin light chain 3. (novusbio.com)
  • Here, using high spatiotemporal imaging of living cells, we quantitatively assessed the architecture and dynamic behavior of cortical actin arrays in a mutant with three Myosin XI ( XI-1 , XI-2 , and XI-K ) genes knocked out ( xi3KO ). (plantphysiol.org)
  • The conversion of chemical energy to mechanical energy is intervened by changes in the myosin shape leading to ATP binding to the actin. (differencebetween.net)
  • Unconventional myosins serve in intracellular movements. (abcam.com)
  • Calcium inhibition as an intracellular signal for actin-myosin interaction. (thefreelibrary.com)
  • Plant cell expansion relies on intracellular trafficking of vesicles and macromolecules, which requires myosin motors and a dynamic actin network. (plantphysiol.org)
  • [5] The power stroke occurs at the release of phosphate from the myosin molecule after the ATP hydrolysis while myosin is tightly bound to actin. (wikipedia.org)
  • The release of the ADP molecule leads to the so-called rigor state of myosin. (wikipedia.org)
  • [6] The binding of a new ATP molecule will release myosin from actin. (wikipedia.org)
  • Binding of a new molecule of ATP to myosin head triggers it to let go of actin and the cycle starts all over again. (wikibooks.org)
  • The myosin V structure reveals at atomic resolution how the major cleft in the molecule closes and leads to a new actin-binding interface. (esrf.eu)
  • The thick filament is composed of what molecule MYOSIN b. (majortests.com)
  • Which molecule has a binding site for myosin heads ACTIN b. (majortests.com)
  • What molecule must bind to the myosin head in order for it to disconnect with Actin ATP 5. (majortests.com)
  • Hydrolysis of the molecule in question 4 returns the myosin molecule to the HIGH ENERGY confirmation. (majortests.com)
  • Myosin is a molecule-sized muscle that uses chemical energy to perform motions. (sciencephoto.com)
  • Human Usher Ib/mouse shaker-1: the retinal phenotype discrepancy explained by the presence/absence of myosin VIIA in the photoreceptor cells. (nature.com)
  • Myosin VIIA mutation screening in 189 Usher syndrome type 1 patients. (nature.com)
  • In retina, myosin VIIa may play a role in trafficking of ribbon-synaptic vesicle complexes and renewal of the outer photoreceptors disks. (abcam.com)
  • Detects Myosin VIIa from mouse tissues as well as recombinant. (abcam.com)
  • Synthetic peptide corresponding to Mouse Myosin VIIa aa 16-31. (abcam.com)
  • Detects a band of approximately 220 kDa.Can be blocked with Myosin VIIa peptide (ab4996) . (abcam.com)
  • Skeletal muscle myosin, the most conspicuous of the myosin superfamily due to its abundance in muscle fibers , was the first to be discovered. (wikipedia.org)
  • Virtually all eukaryotic cells contain myosin isoforms . (wikipedia.org)
  • Specific nuclear localizing sequence directs two myosin isoforms to the cell nucleus in calmodulin-sensitive manner. (springer.com)
  • Tissue specific expression of Myosin IC Isoforms. (springer.com)
  • Mouse nuclear myosin I knock-out shows interchangeability and redundancy of myosin isoforms in the cell nucleus. (springer.com)
  • The expression of myosin heavy-chain (MyHC) isoforms is developmentally regulated. (gu.se)
  • The myosin heavy chain (MyHC) isoforms are the best molecular markers of functional heterogeneity of muscle fibers. (diva-portal.org)
  • The head domain binds the filamentous actin , and uses ATP hydrolysis to generate force and to "walk" along the filament towards the barbed (+) end (with the exception of myosin VI, which moves towards the pointed (-) end). (wikipedia.org)
  • BACKGROUND: Myosin is a molecular motor and the essential part of the thick filament of striated muscle. (gu.se)
  • 6. Binding of the myosin heads sequentially prevents CROSS BRIDGE BINDING of the thin filament. (majortests.com)
  • Sliding Filament Theory and Muscle Tissues study guide Front Back Binding of the myosin head sequentailly prevents "_____________" of the thin filament. (majortests.com)
  • The A band is the length of myosin filament. (differencebetween.net)
  • The M line is the central myosin filament thickening. (differencebetween.net)
  • The calcium ions are the one setting off the binding of myosin to actin commencing filament sliding. (differencebetween.net)
  • Myosin filament assembly in an ever-changing myofilament lattice of smooth muscle. (semanticscholar.org)
  • M-region structure and myosin filament symmetry. (semanticscholar.org)
  • Thus, our data provide genetic evidence that three Arabidopsis class XI myosins contribute to actin remodeling by stimulating turnover and generating the force for filament shape change. (plantphysiol.org)
  • Myosin motors interact with filamentous actin (F-actin) to form complex arrays such as the contractile ring driving cell division ( 3 , 4 ) and contractile networks that drive cell migration ( 4 ) and polarizing cortical flows ( 5 , 6 ). (pnas.org)
  • Fig. 23: Structural states of myosin during the contractile cycle. (esrf.eu)
  • Cell division concludes with cytokinesis, a process driven by a contractile ring of actin and myosin that lies underneath the plasma membrane at the cell's equator. (biologists.org)
  • ABSTRACT We propose a molecular mechanism of force generation in muscle, based primarily on site-specific spectroscopic probe studies of myosin heads in contracting muscle fibers and myofibrils. (majortests.com)
  • ADP dissociation leaves the myosin head tightly bound to actin. (wikibooks.org)
  • 1-Without bound nucleotide, myosin is strongly bound to actin (rigor state). (esrf.eu)
  • 5- Myosin is again strongly bound to actin without nucleotide bound. (esrf.eu)
  • However, since force production occurs when myosin is strongly bound to actin, details of the strongly-bound states of myosin are essential to understand how force is produced. (esrf.eu)
  • The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription. (springer.com)
  • Myosin-1c interacts with hair-cell receptors through its calmodulin-binding IQ domains. (springer.com)
  • Interacts with calmodulin (CMD1) and the myosin light chain MLC1 through its IQ repeats. (rcsb.org)
  • MYL6B usually interacts with Myosin Va, an Actin based motor which moves in large steps. (prospecbio.com)
  • Anderson BL, Boldogh I, Evangelista M, Boone C, Greene LA, Pon LA. The Src homology domain 3 (SH3) of a yeast type I myosin, Myo5p, binds to verprolin and is required for targeting to sites of actin polarization. (springer.com)
  • In this publication, the authors demonstrated that omecamtiv mecarbil binds to the myosin catalytic domain and acts by an allosteric mechanism to increase the transition rate of myosin into the strongly actin-bound force-generating state. (redorbit.com)
  • In cells, many vital processes involve myosin-driven motility that actively remodels the actin cytoskeleton and changes cell shape. (pnas.org)
  • In Toxoplasma gondii , in particular, motility and host cell invasion are powered by the parasite actin cytoskeleton and most likely by myosin motors ( Dobrowolski and Sibley, 1996 ). (rupress.org)
  • Type I myosins are thought to drive actin-dependent membrane motility, but the direct demonstration in vivo of their involvement in specific cellular processes has been difficult. (sciencemag.org)
  • 1992), little or no information about the functional role of myosins in growth cone motility has emerged (cf Tanaka and Sabry, 1995). (thefreelibrary.com)
  • Unconventional myosins are also critical for motility in amoeba and a mammalian paralog (Myo1C) is critical as a glucose transporter that recycles glucose in response to insulin. (rockland-inc.com)
  • Arabidopsis ( Arabidopsis thaliana ) myosin XI powers the motility of diverse cellular organelles, including endoplasmic reticulum, Golgi, endomembrane vesicles, peroxisomes, and mitochondria. (plantphysiol.org)
  • Myosin is both a motor that drives long-distance cargo motility and also an actin regulator. (plantphysiol.org)
  • Binding of calcium ion to this domain increases the affinity of MYLK binding to myosin light chain. (wikipedia.org)
  • The structure and function of myosin is globally conserved across species, to the extent that rabbit muscle myosin II will bind to actin from an amoeba . (wikipedia.org)
  • These new myosins were collectively termed "unconventional myosins" [7] and have been found in many tissues other than muscle. (wikipedia.org)
  • Myosin storage myopathy is a condition that causes muscle weakness (myopathy) that does not worsen or worsens very slowly over time. (medlineplus.gov)
  • It is unclear how these changes lead to muscle weakness in people with myosin storage myopathy. (medlineplus.gov)
  • The actin is in the middle of the muscle, and the myosin is attached to the sides of the muscles so it can't move. (smore.com)
  • When this happens we have what are called Z disks in our muscles and when the actin starts to slide past the myosin the z disks move closer and closer together and now the muscle is contracted. (smore.com)
  • This year's squad has a large number of medics and biologists in the squad, so CUWBC chose to named their crews Actin and Myosin after the two muscle fibers that pull against each other in the human body. (theboatrace.org)
  • Sequence analysis revealed that one cDNA fragment represented the myosin alkali light chain (MLC 1sm) of human smooth muscle. (ingentaconnect.com)
  • When myosin and actin are combined together, that makes the muscle produce force. (wikibooks.org)
  • PURPOSE: To investigate the myosin heavy chain (MyHC) composition of human extraocular (EOM) and levator palpebrae (LP) muscle fibers. (diva-portal.org)
  • Computer artwork of the molecular actin myosin muscle structure. (sciencephoto.com)
  • Electron paramagnetic resonance (EPR) and timeresolved phosphorescence anisotropy (TPA) of probes attached to SH1 (Cys 707, in the catalytic domain of the head) have consistently shown that most myosin heads in contracting muscle are dynamically disordered, undergoing large-amplitude rotations in the ps time range. (majortests.com)
  • Myosin Light Chain 6B (MYL6B) is a heavy chain regulator located in smooth muscle and non-muscle Myosin complexes. (prospecbio.com)
  • About 20 classes of myosin have been distinguished on the basis of the sequence of amino acids in their ATP-hydrolyzing motor domains. (wikibooks.org)
  • There are 20 different types of Myosin that already distinguished by amino acid sequence. (wikibooks.org)
  • Myosins can be divided into classes that are distinguished based on sequence features of the motor, or head domain, but also have distinct tail regions that are believed to bind specific cargoes. (rockland-inc.com)
  • A BLAST analysis was used to suggest cross reactivity with Myosin 1G from human, mouse, chimpanzee and rat based on 100% homology with the immunizing sequence. (rockland-inc.com)
  • Revisiting Myosin Families Through Large-scale Sequence Searches Leads to the Discovery of New Myosins. (ncbs.res.in)
  • Computational search algorithms were performed to identify putative myosin members by phylogenetic analysis, sequence motifs, and coexisting domains. (ncbs.res.in)
  • The signs and symptoms of myosin storage myopathy usually become noticeable in childhood, although they can occur later. (medlineplus.gov)
  • Myosin storage myopathy is a rare condition. (medlineplus.gov)
  • Tajsharghi H, Thornell LE, Lindberg C, Lindvall B, Henriksson KG, Oldfors A. Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. (medlineplus.gov)
  • Myosin I: from yeast to human. (springer.com)
  • An ordered array of yeast artificial chromosome clones that encompasses the Dictyostelium genome was probed at low stringency with conserved regions of the myosin motor domain to identify all possible myosin loci. (pnas.org)
  • The previously identified myosin loci (mchA, myoA-E) were detected by hybridization to the probes, as well as an additional seven previously unidentified loci (referred to as myoF-L). Clones corresponding to four of these additional loci (myoF, myoH-J) were obtained by using the isolated yeast artificial chromosomes as templates in a PCR employing degenerate primers specific for conserved regions of the myosin head. (pnas.org)
  • Evidence from yeast secretory vesicles and mitochondria, and mammalian melanosomes and endosomes suggests that Rab GTPases are crucial components of the myosin organelle receptor machinery. (ovid.com)
  • Differential localization and dynamics of class I myosins in the enterocyte microvillus. (springer.com)
  • Cloning and chromosomal localization of a human class III myosin. (ebi.ac.uk)
  • 1993) and localization of myosins to growth cones (Rochlin et al. (thefreelibrary.com)
  • We elucidated a role for myosin Va (MyoVa) to modulate the axonal localization and transport of ZBP1 in axons. (jneurosci.org)
  • We hypothesized that the prominent brain myosin MyoVa can modulate the axonal localization and transport of ZBP1. (jneurosci.org)
  • 4 A second was the elucidation of the functional domains of MLCP, 5 which consist of a 37-kDa catalytic subunit, a 20-kDa subunit of unknown function, and a 110- to 130-kDa subunit that targets MLCP to myosin. (ahajournals.org)
  • Therefore, it has been proposed that the catalytic domain of the myosin head has only one stereospecific (rigor-like) actin-binding angle, and that the head's internal structure changes during force generation, causing the distal light-chain-binding domain to rotate. (majortests.com)
  • We expressed and crystallised a class V myosin containing only a motor domain and the first calmodulin-binding site (first part of the lever arm). (esrf.eu)
  • The physical mechanism of self-organization in the actin-myosin cytoskeleton remains unknown. (pnas.org)
  • A myosin light chain is a light chain (small polypeptide subunit) of myosin. (wikipedia.org)
  • Myosin IIA-related Actomyosin Contractility Mediates Oxidative Stress-induced Neuronal Apoptosis. (sigmaaldrich.com)