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.
Myosin Heavy Chains
Myosin Type II
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).
Myosin Light Chains
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.
Myosin Type V
Nonmuscle Myosin Type IIA
Myosin Type I
Nonmuscle Myosin Type IIB
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.
Myosin Type III
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.
Heterocyclic Compounds with 4 or More Rings
Molecular Motor Proteins
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 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.
Muscle Fibers, Skeletal
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.
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.
Amino Acid Sequence
Molecular Sequence Data
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.
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.
Electrophoresis, Polyacrylamide Gel
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.
Myosin Type IV
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).
Muscle Fibers, Slow-Twitch
Muscle Fibers, Fast-Twitch
Protein Structure, Tertiary
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.
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.
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.
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)
MBInfo - Myosin Isoforms MBInfo - The Myosin Powerstroke Myosin Video A video of a moving myosin motor protein. Myosins at the ... Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be ... Myosin VI is thought to transport endocytic vesicles into the cell. Myosin VII is an unconventional myosin with two FERM ... Myosin II (also known as conventional myosin) is the myosin type responsible for producing muscle contraction in muscle cells ...
... is a protein that in humans is encoded by the MYH11 gene. Myosin-11 is a smooth muscle myosin belonging to the myosin ... Chicken Myosin-11) at the PDBe-KB. Babu GJ, Warshaw DM, Periasamy M (2000). "Smooth muscle myosin heavy chain isoforms and ... Myosin-11 is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light ... Actin, desmin, myosin, and tropomyosin". Am. J. Pathol. 142 (1): 221-30. PMC 1886840. PMID 8424456. New L, Jiang Y, Zhao M, et ...
"The sequence of the myosin 50-20K loop affects Myosin's affinity for actin throughout the actin-myosin ATPase cycle and its ... Myosin Rayment I (July 1996). "The structural basis of the myosin ATPase activity". The Journal of Biological Chemistry. 271 ( ... Myosin ATPase (EC 18.104.22.168) is an enzyme with systematic name ATP phosphohydrolase (actin-translocating). This enzyme catalyses ... Myosin+ATPase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with short ...
The myosin head is the part of the thick myofilament made up of myosin that acts in muscle contraction, by sliding over thin ... Myosin is the major component of the thick filaments and most myosin molecules are composed of a head, neck, and tail domain; ... The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed. ... There are many cell-specific isoforms of myosin heavy chains, coded for by a multi-gene family. Myosin interacts with actin to ...
... (myosin heavy chain 2) is a protein that in humans is encoded by the MYH2 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: MYH2 myosin, heavy chain 2, skeletal muscle, adult". Schwartz CE, McNally E, Leinwand L, Skolnick MH (1987). "A ... 2002). "Myosin heavy chain IIa gene mutation E706K is pathogenic and its expression increases with age". Neurology. 58 (5): 780 ... Chung MC, Kawamoto S (2005). "IRF-2 is involved in up-regulation of nonmuscle myosin heavy chain II-A gene expression during ...
Myosins are actin-dependent motor proteins and are categorized into conventional myosins (class II) and unconventional myosins ... Myosin-IIIa is a protein that in humans is encoded by the MYO3A gene. The protein encoded by this gene belongs to the myosin ... "Entrez Gene: MYO3A myosin IIIA". Walsh T, Walsh V, Vreugde S, et al. (2002). "From flies' eyes to our ears: mutations in a ... Class III myosins, such as this one, have a kinase domain N-terminal to the conserved N-terminal motor domains and are ...
Rodriguez OC, Cheney RE (Mar 2002). "Human myosin-Vc is a novel class V myosin expressed in epithelial cells". Journal of Cell ... Myosin Va is highly expressed in the nervous system and it is present in almost the entire brain. MY5A perform an important ... Defects in Myosin Va are associated with Griscelli syndrome type 1, also known as Elejalde syndrome a rare autosomal recessive ... Myosin Va is highly expressed in neurons and melanocytes. MYO5A has been shown to interact with DYNLL1, RAB27A, DYNLL2, ...
... , is a protein that in humans is coded for by MYO6. Unconventional myosin-VI is a myosin molecular ... Myosin-VI's Met-Ile-Sec bonding interactions are limited to the myosin-VI long isoform but interact with clathrin in ... Human myosin-VI contains a N-terminal myosin head domain (residues 59-759), two coiled coil motifs (residues 902-984 and 986- ... Myosin-VI follows the same structure as other myosin but with two unique "inserts" allowing for its diversified properties. One ...
Myosin light chain
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 ( ...
Skowron JF, Bement WM, Mooseker MS (1999). "Human brush border myosin-I and myosin-Ic expression in human intestine and Caco- ... The protein encoded by this gene belongs to the myosin superfamily. Myosins are molecular motors that, upon interaction with ... and/or enzymatic activities and targets each myosin to its particular subcellular location. The myosin-Ia protein is expressed ... Each myosin has a conserved N-terminal motor domain that contains both ATP-binding and actin-binding sequences. Following the ...
Myosin light chain 5
This gene encodes one of the myosin light chains, a component of the hexameric ATPase cellular motor protein myosin. Myosin is ... "Entrez Gene: Myosin light chain 5". Retrieved 2017-01-24. This article incorporates text from the United States National ... Myosin light chain 5 is a protein that, in humans, is encoded by the MYL5 gene. ...
Myosin light-chain kinase
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 ...
When myosin phosphatase binds to myosin, it removes the phosphate group. Without the group, the myosin reverts to its original ... Myosin light-chain phosphatase, also called myosin phosphatase (EC 22.214.171.124; systematic name [myosin-light-chain]-phosphate ... that dephosphorylates the regulatory light chain of myosin II: [myosin light-chain] phosphate + H2O = [myosin light-chain] + ... Myosin II, also known as conventional myosin, has two heavy chains that consist of the head and tail domains and four light ...
... calmodulin-dependent myosin heavy chain kinase MHCK MIHC kinase myosin heavy chain kinase myosin I heavy-chain kinase myosin II ... In enzymology, a myosin-heavy-chain kinase (EC 126.96.36.199) is an enzyme that catalyzes the chemical reaction ATP + [myosin heavy- ... kinase myosin heavy chain kinase A STK6. Cote GP, Bukiejko U (1987). "Purification and characterization of a myosin heavy chain ... the two substrates of this enzyme are ATP and myosin heavy-chain, whereas its two products are ADP and myosin heavy-chain ...
Myosin binding protein C, cardiac
"Dissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. Structure and myosin binding of domain ... cMyBP-C regulates the positioning of myosin and actin for interaction and acts as a tether to the myosin S1 heads, limiting ... cMyBP-C is a myosin-associated protein that binds at 43 nm intervals along the myosin thick filament backbone, stretching for ... Harris SP, Rostkova E, Gautel M, Moss RL (Oct 2004). "Binding of myosin binding protein-C to myosin subfragment S2 affects ...
Myosin viia and rab interacting protein
... is a protein that in humans is encoded by the MYRIP gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Myosin VIIA and Rab interacting protein". Retrieved 2016-03-29. El-Amraoui A, Schonn JS, Küssel-Andermann P, ... Blanchard S, Desnos C, Henry JP, Wolfrum U, Darchen F, Petit C (2002). "MyRIP, a novel Rab effector, enables myosin VIIa ...
Misato segment II myosin-like domain
A comparison of segment II with the vertebrate myosin heavy chains reveals that it is homologous to a myosin peptide in the ... The most significant sequence similarities to this 54-amino acid region are from a motif found in the heavy chains of myosins ... Segments I and III are common to tubulins (INTERPRO), but segment II aligns with myosin heavy chain sequences from Drosophila ... Segment II also contains heptad repeats which are characteristic of the myosin tail alpha-helical coiled-coils. Kimura M, Okano ...
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 ...
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 IIs are motor proteins that are part of a superfamily composed of more than 30 classes. Class II myosins include muscle ... The path to myosin filament formation, which is shared by NM II and smooth muscle myosin, starts with a folded inactive ... April 2010). "Heavy chain myosin 9-related disease (MYH9 -RD): neutrophil inclusions of myosin-9 as a pathognomonic sign of the ...
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. 17 (8): 878-90. doi:10.1111/tra.12410. PMC ... Kruppa AJ, Kendrick-Jones J, Buss F (2016). "Myosins, Actin and Autophagy". Traffic. 17 (8): 878-90. doi:10.1111/tra.12410. PMC ...
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 ...
Kielley WW (1961). "Myosin adenosine triphosphatase". In Boyer PD, Lardy H, Myrbäck K (eds.). The Enzymes. Vol. 5 (2nd ed.). ... myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold". EMBO J. 1 (8): 945-51. doi:10.1002/j. ...
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 ...
The first identified myosin, myosin II, is responsible for generating muscle contraction. Myosin II is an elongated protein ... Because myosin II is essential for muscle contraction, defects in muscular myosin predictably cause myopathies. Myosin is ... The myosin heads bind and hydrolyze ATP, which provides the energy to walk toward the plus end of an actin filament. Myosin II ... In addition to myosin II, many other myosin types are responsible for variety of movement of non-muscle cells. For example, ...
It is the enzymatic activity of the ATPase in the myosin head that cyclically hydrolyzes ATP, fueling the myosin power stroke. ... MYH7 is a gene encoding a myosin heavy chain beta (MHC-β) isoform (slow twitch) expressed primarily in the heart, but also in ... Harris SP, Lyons RG, Bezold KL (March 2011). "In the thick of it: HCM-causing mutations in myosin binding proteins of the thick ... An accepted mechanism for this process is that ADP-bound myosin attaches to actin while thrusting tropomyosin inwards, then the ...
Hodge T, Cope M (1 October 2000). "A myosin family tree". J Cell Sci. 113 (19): 3353-4. doi:10.1242/jcs.113.19.3353. PMID ... National Science Foundation's Assembling the Tree of Life Project PhyloCode A Multiple Alignment of 139 Myosin Sequences and a ...
List of OMIM disorder codes
... myosin storage; 608358; MYH7 Myopathy, nemaline, 3; 161800; ACTA1 Myopathy, proximal, with early respiratory muscle involvement ...
The Boat Race 2020
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 ...
Berg JS, Powell BC, Cheney RE (April 2001). "A millennial myosin census". Molecular Biology of the Cell. 12 (4): 780-94. doi: ... They also generate movement, with myosin hydrolyzing ATP to generate muscle contraction, and also transport cargo around the ...