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.
Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.
A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. They remodel the actin CYTOSKELETON by severing ACTIN FILAMENTS and increasing the rate of monomer dissociation.
Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
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.
Reduced (protonated) form of THIAZOLES. They can be oxidized to THIAZOLIDINEDIONES.
A 90-kDa protein produced by macrophages that severs ACTIN filaments and forms a cap on the newly exposed filament end. Gelsolin is activated by CALCIUM ions and participates in the assembly and disassembly of actin, thereby increasing the motility of some CELLS.
A family of low molecular weight proteins that bind ACTIN and control actin polymerization. They are found in eukaryotes and are ubiquitously expressed.
A fungal metabolite that blocks cytoplasmic cleavage by blocking formation of contractile microfilament structures resulting in multinucleated cell formation, reversible inhibition of cell movement, and the induction of cellular extrusion. Additional reported effects include the inhibition of actin polymerization, DNA synthesis, sperm motility, glucose transport, thyroid secretion, and growth hormone release.
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.
A class of saturated compounds consisting of two rings only, having two or more atoms in common, containing at least one hetero atom, and that take the name of an open chain hydrocarbon containing the same total number of atoms. (From Riguady et al., Nomenclature of Organic Chemistry, 1979, p31)
A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments.
Proteins which participate in contractile processes. They include MUSCLE PROTEINS as well as those found in other cells and tissues. In the latter, these proteins participate in localized contractile events in the cytoplasm, in motile activity, and in cell aggregation phenomena.
A dynamic actin-rich extension of the surface of an animal cell used for locomotion or prehension of food.
A protein found in the thin filaments of muscle fibers. It inhibits contraction of the muscle unless its position is modified by TROPONIN.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
A PROFILIN binding domain protein that is part of the Arp2-3 complex. It is related in sequence and structure to ACTIN and binds ATP.
A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. It is expressed at higher levels than ARP2 PROTEIN and does not contain a PROFILIN binding domain.
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.
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.
Chemical reaction in which monomeric components are combined to form POLYMERS (e.g., POLYMETHYLMETHACRYLATE).
A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.
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 protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.
Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS).
Compounds consisting of chains of AMINO ACIDS alternating with CARBOXYLIC ACIDS via ester and amide linkages. They are commonly cyclized.
A member of the Wiskott-Aldrich syndrome protein family that is found at high levels in NERVE CELLS. It interacts with GRB2 ADAPTOR PROTEIN and with CDC42 PROTEIN.
Polymers synthesized by living organisms. They play a role in the formation of macromolecular structures and are synthesized via the covalent linkage of biological molecules, especially AMINO ACIDS; NUCLEOTIDES; and CARBOHYDRATES.
WASP protein is mutated in WISKOTT-ALDRICH SYNDROME and is expressed primarily in hematopoietic cells. It is the founding member of the WASP protein family and interacts with CDC42 PROTEIN to help regulate ACTIN polymerization.
A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC
11- to 14-membered macrocyclic lactones with a fused isoindolone. Members with INDOLES attached at the C10 position are called chaetoglobosins. They are produced by various fungi. Some members interact with ACTIN and inhibit CYTOKINESIS.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
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 member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC
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.
Contractile tissue that produces movement in animals.
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 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.
A family of crosslinking filament proteins encoded by distinct FLN genes. Filamins are involved in cell adhesion, spreading, and migration, acting as scaffolds for over 90 binding partners including channels, receptors, intracellular signaling molecules and transcription factors. Due to the range of molecular interactions, mutations in FLN genes result in anomalies with moderate to lethal consequences.
A cytoskeletal protein associated with cell-cell and cell-matrix interactions. The amino acid sequence of human vinculin has been determined. The protein consists of 1066 amino acid residues and its gene has been assigned to chromosome 10.
A family of microfilament proteins whose name derives from the fact that mutations in members of this protein family have been associated with WISKOTT-ALDRICH SYNDROME. They are involved in ACTIN polymerization and contain a polyproline-rich region that binds to PROFILIN, and a verprolin homology domain that binds G-ACTIN.
The resistance that a gaseous or liquid system offers to flow when it is subjected to shear stress. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
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.
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.
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.
The rate dynamics in chemical or physical systems.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
Specialized structures of the cell that extend the cell membrane and project out from the cell surface.
Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS.
A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Established cell cultures that have the potential to propagate indefinitely.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
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.
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC
A sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. This enzyme was formerly listed as EC
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
A cytotoxic member of the CYTOCHALASINS.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
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.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
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.
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.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Compounds that inhibit cell production of DNA or RNA.
An actin capping protein that binds to the pointed-end of ACTIN. It functions in the presence of TROPOMYOSIN to inhibit microfilament elongation.
An anchoring junction of the cell to a non-cellular substrate. It is composed of a specialized area of the plasma membrane where bundles of the ACTIN CYTOSKELETON terminate and attach to the transmembrane linkers, INTEGRINS, which in turn attach through their extracellular domains to EXTRACELLULAR MATRIX PROTEINS.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
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 quality of surface form or outline of CELLS.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
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 phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
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.
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).
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 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.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Microscopy in which television cameras are used to brighten magnified images that are otherwise too dark to be seen with the naked eye. It is used frequently in TELEPATHOLOGY.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The quantity of volume or surface area of CELLS.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
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).
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A family of 3,6-di(substituted-amino)-9-benzoate derivatives of xanthene that are used as dyes and as indicators for various metals; also used as fluorescent tracers in histochemistry.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
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 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 .
A zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half.
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.
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.
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.
Toxic proteins produced from the species CLOSTRIDIUM BOTULINUM. The toxins are synthesized as a single peptide chain which is processed into a mature protein consisting of a heavy chain and light chain joined via a disulfide bond. The botulinum toxin light chain is a zinc-dependent protease which is released from the heavy chain upon ENDOCYTOSIS into PRESYNAPTIC NERVE ENDINGS. Once inside the cell the botulinum toxin light chain cleaves specific SNARE proteins which are essential for secretion of ACETYLCHOLINE by SYNAPTIC VESICLES. This inhibition of acetylcholine release results in muscular PARALYSIS.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
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.
Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.
A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.
Elements of limited time intervals, contributing to particular results or situations.
Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
The process by which the CYTOPLASM of a cell is divided.
A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE.
An enzyme capable of hydrolyzing highly polymerized DNA by splitting phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide. This catalyzes endonucleolytic cleavage of DNA yielding 5'-phosphodi- and oligonucleotide end-products. The enzyme has a preference for double-stranded DNA.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
A method used to study the lateral movement of MEMBRANE PROTEINS and LIPIDS. A small area of a cell membrane is bleached by laser light and the amount of time necessary for unbleached fluorescent marker-tagged proteins to diffuse back into the bleached site is a measurement of the cell membrane's fluidity. The diffusion coefficient of a protein or lipid in the membrane can be calculated from the data. (From Segen, Current Med Talk, 1995).
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Agents that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.
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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Recording serial images of a process at regular intervals spaced out over a longer period of time than the time in which the recordings will be played back.
An intermediate filament protein found predominantly in smooth, skeletal, and cardiac muscle cells. Localized at the Z line. MW 50,000 to 55,000 is species dependent.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Measurement of the intensity and quality of fluorescence.
Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
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.
Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
The sum of the weight of all the atoms in a molecule.
Proteins found in any species of fungus.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Proteins prepared by recombinant DNA technology.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
A continuous cell line of high contact-inhibition established from NIH Swiss mouse embryo cultures. The cells are useful for DNA transfection and transformation studies. (From ATCC [Internet]. Virginia: American Type Culture Collection; c2002 [cited 2002 Sept 26]. Available from
Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Toxic or poisonous substances elaborated by marine flora or fauna. They include also specific, characterized poisons or toxins for which there is no more specific heading, like those from poisonous FISHES.
The repeating contractile units of the MYOFIBRIL, delimited by Z bands along its length.
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.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
A rare, X-linked immunodeficiency syndrome characterized by ECZEMA; LYMPHOPENIA; and, recurrent pyogenic infection. It is seen exclusively in young boys. Typically, IMMUNOGLOBULIN M levels are low and IMMUNOGLOBULIN A and IMMUNOGLOBULIN E levels are elevated. Lymphoreticular malignancies are common.
An intermediate filament protein found in most differentiating cells, in cells grown in tissue culture, and in certain fully differentiated cells. Its insolubility suggests that it serves a structural function in the cytoplasm. MW 52,000.
Colloids with a solid continuous phase and liquid as the dispersed phase; gels may be unstable when, due to temperature or other cause, the solid phase liquefies; the resulting colloid is called a sol.
Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.
A group of condensed ring hydrocarbons.
Bulbous enlargement of the growing tip of nerve axons and dendrites. They are crucial to neuronal development because of their pathfinding ability and their role in synaptogenesis.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
A nonmuscle isoform of myosin type II found predominantly in platelets, lymphocytes, neutrophils and brush border enterocytes.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
Structures which are part of the CELL MEMBRANE or have cell membrane as a major part of their structure.
A purely physical condition which exists within any material because of strain or deformation by external forces or by non-uniform thermal expansion; expressed quantitatively in units of force per unit area.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
One of two types of muscle in the body, characterized by the array of bands observed under microscope. Striated muscles can be divided into two subtypes: the CARDIAC MUSCLE and the SKELETAL MUSCLE.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
Proteins that are preferentially expressed or upregulated during FETAL DEVELOPMENT.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A GTP-BINDING PROTEIN involved in regulating a signal transduction pathway that controls assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC
Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Minute projections of cell membranes which greatly increase the surface area of the cell.
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 insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.
Microscopy in which the object is examined directly by an electron beam scanning the specimen point-by-point. The image is constructed by detecting the products of specimen interactions that are projected above the plane of the sample, such as backscattered electrons. Although SCANNING TRANSMISSION ELECTRON MICROSCOPY also scans the specimen point by point with the electron beam, the image is constructed by detecting the electrons, or their interaction products that are transmitted through the sample plane, so that is a form of TRANSMISSION ELECTRON MICROSCOPY.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Carbodiimide cross-linking reagent.
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 catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.
The physical characteristics and processes of biological systems.
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.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
Proteins found in any species of protozoan.
The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.
Spindle-shaped cells with characteristic CONTRACTILE PROTEINS and structures that contribute to the WOUND HEALING process. They occur in GRANULATION TISSUE and also in pathological processes such as FIBROSIS.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
The injection of very small amounts of fluid, often with the aid of a microscope and microsyringes.
A family of serine-threonine kinases that bind to and are activated by MONOMERIC GTP-BINDING PROTEINS such as RAC GTP-BINDING PROTEINS and CDC42 GTP-BINDING PROTEIN. They are intracellular signaling kinases that play a role the regulation of cytoskeletal organization.
The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Resistance and recovery from distortion of shape.
A class of organic compounds that contains a naphthalene moiety linked to a sulfonic acid salt or ester.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
A plant genus in the family LILIACEAE generally growing in temperate areas. The word lily is also used in the common names of many plants of other genera that resemble true lilies. True lilies are erect perennial plants with leafy stems, scaly bulbs, usually narrow leaves, and solitary or clustered flowers.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.

Tyrosine phosphorylation is required for actin-based motility of vaccinia but not Listeria or Shigella. (1/20287)

Studies of the actin-based motility of pathogens have provided important insights into the events occurring at the leading edge of motile cells [1] [2] [3]. To date, several actin-cytoskeleton-associated proteins have been implicated in the motility of Listeria or Shigella: vasodilator-stimulated phosphoprotein (VASP), vinculin and the actin-related protein complex of Arp2 and Arp3 [4] [5] [6] [7]. To further investigate the underlying mechanism of actin-tail assembly, we examined the localization of components of the actin cytoskeleton including Arp3, VASP, vinculin and zyxin during vaccinia, Listeria and Shigella infections. The most striking difference between the systems was that a phosphotyrosine signal was observed only at the site of vaccinia actin-tail assembly. Micro-injection experiments demonstrated that a phosphotyrosine protein plays an important role in vaccinia actin-tail formation. In addition, we observed a phosphotyrosine signal on clathrin-coated vesicles that have associated actin-tail-like structures and on endogenous vesicles in Xenopus egg extracts which are able to nucleate actin tails [8] [9]. Our observations indicate that a host phosphotyrosine protein is required for the nucleation of actin filaments by vaccinia and suggest that this phosphoprotein might be associated with cellular membranes that can nucleate actin.  (+info)

Transformation mediated by RhoA requires activity of ROCK kinases. (2/20287)

BACKGROUND: The Ras-related GTPase RhoA controls signalling processes required for cytoskeletal reorganisation, transcriptional regulation, and transformation. The ability of RhoA mutants to transform cells correlates not with transcription but with their ability to bind ROCK-I, an effector kinase involved in cytoskeletal reorganisation. We used a recently developed specific ROCK inhibitor, Y-27632, and ROCK truncation mutants to investigate the role of ROCK kinases in transcriptional activation and transformation. RESULTS: In NIH3T3 cells, Y-27632 did not prevent the activation of serum response factor, transcription of c-fos or cell cycle re-entry following serum stimulation. Repeated treatment of NIH3T3 cells with Y-27632, however, substantially disrupted their actin fibre network but did not affect their growth rate. Y-27632 blocked focus formation by RhoA and its guanine-nucleotide exchange factors Dbl and mNET1. It did not affect the growth rate of cells transformed by Dbl and mNET1, but restored normal growth control at confluence and prevented their growth in soft agar. Y-27632 also significantly inhibited focus formation by Ras, but had no effect on the establishment or maintenance of transformation by Src. Furthermore, it significantly inhibited anchorage-independent growth of two out of four colorectal tumour cell lines. Consistent with these data, a truncated ROCK derivative exhibited weak ability to cooperate with activated Raf in focus formation assays. CONCLUSIONS: ROCK signalling is required for both the establishment and maintenance of transformation by constitutive activation of RhoA, and contributes to the Ras-transformed phenotype. These observations provide a potential explanation for the requirement for Rho in Ras-mediated transformation. Moreover, the inhibition of ROCK kinases may be of therapeutic use.  (+info)

Polarized distribution of Bcr-Abl in migrating myeloid cells and co-localization of Bcr-Abl and its target proteins. (3/20287)

Bcr-Abl plays a critical role in the pathogenesis of Philadelphia chromosome-positive leukemia. Although a large number of substrates and interacting proteins of Bcr-Abl have been identified, it remains unclear whether Bcr-Abl assembles multi-protein complexes and if it does where these complexes are within cells. We have investigated the localization of Bcr-Abl in 32D myeloid cells attached to the extracellular matrix. We have found that Bcr-Abl displays a polarized distribution, colocalizing with a subset of filamentous actin at trailing portions of migrating 32D cells, and localizes on the cortical F-actin and on vesicle-like structures in resting 32D cells. Deletion of the actin binding domain of Bcr-Abl (Bcr-AbI-AD) dramatically enhances the localization of Bcr-Abl on the vesicle-like structures. These distinct localization patterns of Bcr-Abl and Bcr-Abl-AD enabled us to examine the localization of Bcr-Abl substrate and interacting proteins in relation to Bcr-Abl. We found that a subset of biochemically defined target proteins of Bcr-Abl redistributed and co-localized with Bcr-Abl on F-actin and on vesicle-like structures. The co-localization of signaling proteins with Bcr-Abl at its sites of localization supports the idea that Bcr-Abl forms a multi-protein signaling complex, while the polarized distribution and vesicle-like localization of Bcr-Abl may play a role in leukemogenesis.  (+info)

Evidence for F-actin-dependent and -independent mechanisms involved in assembly and stability of the medial actomyosin ring in fission yeast. (4/20287)

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)

Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. (5/20287)

Recent results have shown that the ability of farnesyltransferase inhibitors (FTIs) to inhibit malignant cell transformation and Ras prenylation can be separated. We proposed previously that farnesylated Rho proteins are important targets for alternation by FTIs, based on studies of RhoB (the FTI-Rho hypothesis). Cells treated with FTIs exhibit a loss of farnesylated RhoB but a gain of geranylgeranylated RhoB (RhoB-GG), which is associated with loss of growth-promoting activity. In this study, we tested whether the gain of RhoB-GG elicited by FTI treatment was sufficient to mediate FTI-induced cell growth inhibition. In support of this hypothesis, when expressed in Ras-transformed cells RhoB-GG induced phenotypic reversion, cell growth inhibition, and activation of the cell cycle kinase inhibitor p21WAF1. RhoB-GG did not affect the phenotype or growth of normal cells. These effects were similar to FTI treatment insofar as they were all induced in transformed cells but not in normal cells. RhoB-GG did not promote anoikis of Ras-transformed cells, implying that this response to FTIs involves loss-of-function effects. Our findings corroborate the FTI-Rho hypothesis and demonstrate that gain-of-function effects on Rho are part of the drug mechanism. Gain of RhoB-GG may explain how FTIs inhibit the growth of human tumor cells that lack Ras mutations.  (+info)

Association of a myosin immunoanalogue with cell envelopes of Aspergillus fumigatus conidia and its participation in swelling and germination. (6/20287)

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)

Yops of Yersinia enterocolitica inhibit receptor-dependent superoxide anion production by human granulocytes. (7/20287)

The virulence plasmid-borne genes encoding Yersinia adhesin A (YadA) and several Yersinia secreted proteins (Yops) are involved in the inhibition of phagocytosis and killing of Yersinia enterocolitica by human granulocytes. One of these Yops, YopH, dephosphorylates multiple tyrosine-phosphorylated proteins in eukaryotic cells and is involved in the inhibition of phagocytosis of Y. enterocolitica by human granulocytes. We investigated whether antibody- and complement-opsonized plasmid-bearing (pYV+) Y. enterocolitica inhibits O2- production by human granulocytes in response to various stimuli and whether YopH is involved. Granulocytes were preincubated with mutant strains unable to express YadA or to secrete Yops or YopH. O2- production by granulocytes during stimulation was assessed by measuring the reduction of ferricytochrome c. PYV+ Y. enterocolitica inhibited O2- production by granulocytes incubated with opsonized Y. enterocolitica or N-formyl-Met-Leu-Phe (f-MLP). This inhibitory effect mediated by pYV did not affect receptor-independent O2- production by granulocytes in response to phorbol myristate acetate, indicating that NADPH activity remained unaffected after activation of protein kinase C. The inhibition of f-MLP-induced O2- production by granulocytes depends on the secretion of Yops and not on the expression of YadA. Insertional inactivation of the yopH gene abrogated the inhibition of phagocytosis of antibody- and complement-opsonized Y. enterocolitica by human granulocytes but not of the f-MLP-induced O2- production by granulocytes or tyrosine phosphorylation of granulocyte proteins. These findings suggest that the specific targets for YopH are not present in f-MLP receptor-linked signal transduction and that other Yop-mediated mechanisms are involved.  (+info)

An RNA switch at the 5' splice site requires ATP and the DEAD box protein Prp28p. (8/20287)

Pre-mRNA splicing requires dramatic RNA rearrangements hypothesized to be catalyzed by ATP-dependent RNA unwindases of the DExD/H box family. In a rearrangement critical for the fidelity of 5' splice site recognition, a base-pairing interaction between the 5' splice site and U1 snRNA must be switched for a mutually exclusive interaction between the 5' splice site and U6 snRNA. By lengthening the U1:5' splice site duplex, we impeded this switch in a temperature-dependent manner and prevented formation of the spliceosome's catalytic core. Using genetics, we identified the DExD/H box protein Prp28p as a potential mediator of the switch. In vitro, the switch requires both Prp28p and ATP. We propose that Prp28p directs isomerization of RNA at the 5' splice site and promotes fidelity in splicing.  (+info)

Pure actin used in research and drug discovery, active actin, actin assay, pyrene actin, fluorescent actin, rhodamine actin, hilyte actin, alexa fluor actin, biotin actin, actin, Actin Protein, Arp2/3 protein, Arp2, Arp3, arp2/3 complex, arp2/3 assay, cofilin, profilin, fodrin, spectrin, tropomyosin, tropomodulin, myosin, actin buffer, actin polymerization buffer, actin cytoskeleton, actin binding proteins, filamin, alpha-actinin, gelsolin.
The heart is a dynamic organ that is made up of multiple cell types including muscle and non-muscle. In general the heart is capable of changing due to many factors including development, physiological response, and pathological conditions. Fibrotic (scarring) and hypertrophic (increase in cell size) diseases of the heart are often associated with messengers (such as calcium (Ca2+)) and pathways that activate proteins normally expressed only in the developing heart. One of these proteins, vascular smooth muscle alpha actin (SMA), is the predominant actin in smooth muscle, but is not normally expressed in the adult heart. However, SMA is activated in response to heart transplant and the associated rejection process (fetal reactivation). The focus of this project is to determine the role of Ca2+ in the regulation of SMA in resident non-muscle cell types of the heart. By using cultured cells we have determined that Ca2+ levels and/or Ca2+ agonists effect previously identified transcription factors ...
Cardiac hypertrophy triggered by mechanical load possesses features in common with growth factor signal transduction. A hemodynamic load provokes rapid expression of the growth factor-inducible nuclear oncogene, c-fos, and certain peptide growth factors specifically stimulate the fetal cardiac genes associated with hypertrophy, even in the absence of load. These include the gene encoding vascular smooth muscle alpha-actin, the earliest alpha-actin expressed during cardiac myogenesis; however, it is not known whether reactivation of the smooth muscle alpha-actin gene occurs in ventricular hypertrophy. We therefore investigated myocardial expression of the smooth muscle alpha-actin gene after hemodynamic overload. Smooth muscle alpha-actin mRNA was discernible 24 h after coarctation and was persistently expressed for up to 30 d. In hypertrophied hearts, the prevalence of smooth muscle alpha-actin gene induction was 0.909, versus 0.545 for skeletal muscle alpha-actin (P less than 0.05). ...
Actin, alpha skeletal muscle is a protein that in humans is encoded by the ACTA1 gene. Actin alpha 1 which is expressed in skeletal muscle is one of six different actin isoforms which have been identified. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus. Skeletal alpha actin expression is induced by stimuli and conditions known to cause muscle formation. Such conditions result in fusion of committed cells (satellite cells) into myotubes, to form muscle fibers. Skeletal actin itself, when expressed, causes expression of several other myogenic genes, which are essential to muscle formation. One key transcription factor that activates skeletal actin gene expression is Serum Response Factor (SRF), a protein that binds to specific sites on the promoter DNA of the actin gene. SRF may bring a number of other proteins to the promoter of skeletal actin, such as andogen receptor, and ...
More than 200 mutations in the skeletal muscle α-actin gene (ACTA1) cause either dominant or recessive skeletal muscle disease. Currently, there are no specific therapies. Cardiac α-actin is 99% identical to skeletal muscle α-actin and the predominant actin isoform in fetal muscle. We previously showed cardiac α-actin can substitute for skeletal muscle α-actin, preventing the early postnatal death of Acta1 knock-out mice, which model recessive ACTA1 disease. Dominant ACTA1 disease is caused by the presence of poison mutant actin protein. Experimental and anecdotal evidence nevertheless indicates that the severity of dominant ACTA1 disease is modulated by the relative amount of mutant skeletal muscle α-actin protein present. Thus, we investigated whether transgenic over-expression of cardiac α-actin in postnatal skeletal muscle could ameliorate the phenotype of mouse models of severe dominant ACTA1 disease. In one model, lethality of ACTA1(D286G). Acta1(+/-) mice was reduced from ∼59% before
Muscle disease caused by mutations in the skeletal muscle alpha-actin gene (ACTA1). Neuromuscul Disord. 2003 Sep; 13(7-8):519-31 ...
ACTC1 encodes cardiac muscle alpha actin. This isoform differs from the alpha actin that is expressed in skeletal muscle, ACTA1. Alpha cardiac actin is the major protein of the thin filament in cardiac sarcomeres, which are responsible for muscle contraction and generation of force to support the pump function of the heart. Cardiac alpha actin is a 42.0 kDa protein composed of 377 amino acids. Cardiac alpha actin is a filamentous protein extending from a complex mesh with cardiac alpha-actinin (ACTN2) at Z-lines towards the center of the sarcomere. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to four others. The atomic structure of monomeric actin was solved by Kabsch et al., and closely thereafter this same group published the structure of the actin filament. Actins are highly conserved proteins; the alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. ...
TY - JOUR. T1 - Actin Filament Bundling and Different Nucleating Effects of Mouse Diaphanous-Related Formin FH2 Domains on Actin/ADF and Actin/Cofilin Complexes. AU - Machaidze, Gia. AU - Sokoll, Andrea. AU - Shimada, Atsushi. AU - Lustig, Ariel. AU - Mazur, Antonina. AU - Wittinghofer, Alfred. AU - Aebi, Ueli. AU - Mannherz, Hans Georg. PY - 2010/11/5. Y1 - 2010/11/5. N2 - Mouse Diaphanous-related formins (mDias) are members of the formin protein family that nucleate actin polymerization and subsequently promote filamentous actin (F-actin) elongation by monomer addition to fast-growing barbed ends. It has been suggested that mDias preferentially recruit actin complexed to profilin due to their proline-rich FH1 domains. During filament elongation, dimeric mDias remain attached to the barbed ends by their FH2 domains, which form an anti-parallel ring-like structure enclosing the filament barbed ends. Dimer formation of mDia-FH2 domains is dependent on their N-terminal lasso and linker subdomains ...
TY - JOUR. T1 - WASH phosphorylation balances endosomal versus cortical actin network integrities during epithelial morphogenesis. AU - Tsarouhas, Vasilios. AU - Liu, Dan. AU - Tsikala, Georgia. AU - Fedoseienko, Alina. AU - Zinn, Kai. AU - Matsuda, Ryo. AU - Billadeau, Daniel D.. AU - Samakovlis, Christos. PY - 2019/12/1. Y1 - 2019/12/1. N2 - Filamentous actin (F-actin) networks facilitate key processes like cell shape control, division, polarization and motility. The dynamic coordination of F-actin networks and its impact on cellular activities are poorly understood. We report an antagonistic relationship between endosomal F-actin assembly and cortical actin bundle integrity during Drosophila airway maturation. Double mutants lacking receptor tyrosine phosphatases (PTP) Ptp10D and Ptp4E, clear luminal proteins and disassemble apical actin bundles prematurely. These defects are counterbalanced by reduction of endosomal trafficking and by mutations affecting the tyrosine kinase Btk29A, and the ...
Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of the filament to polymerize and depolymerize at its ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. Here, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by proteins that bind to the lateral filament surface. We also show that the less dynamic end, called the pointed-end, has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of filament flexibility and Brownian dynamics simulations suggest that the observed kinetic diversity arises from structural alteration. Tuning filament kinetics by exploiting the natural malleability of the actin filament structure may be a ubiquitous mechanism to generate the ...
The current evidence suggests that c-Abl and Arg kinases are activated and recruited by different extracellular stimuli to regulate distinct F-actin structures. Progress has been made in understanding the mechanisms of c-Abl activation by growth factors and the ECM, and in identifying some of the substrates or collaborators of c-Abl in regulating the F-actin cytoskeleton. Because c-Abl is involved in several different F-actin-dependent processes, it is likely to collaborate with other F-actin regulators to determine the dynamic biological output. Multi-protein complexes containing c-Abl or c-Abl substrates may have specific subcellular localization to regulate distinct F-actin structures in various F-actin-dependent processes. Further investigation is now required to characterize the key upstream components in c-Abl cytoskeletal signaling pathways. Moreover, it is important to determine precisely when, where and why the crucial c-Abl substrates are phosphorylated and how this affects the ...
Branched actin networks harness the free energy of actin filament assembly to generate forces required for many important cellular processes (Pollard & Cooper, 2009; Blanchoin et al, 2014). These self‐assembling, cytoskeletal structures push against loads (generally cellular membranes) by promoting nucleation and elongation of actin filaments near the load surface (Pollard et al, 2000). Filament nucleation in branched networks is controlled by membrane‐associated signaling molecules, which recruit nucleation‐promoting factors (NPFs) that, in turn, localize the Arp2/3 complex and stimulate its actin nucleation activity (Pollard et al, 2000; Rotty et al, 2013). Filament elongation near the membrane surface is generally assumed to occur via diffusion‐limited incorporation of actin monomers directly from solution (Pollard et al, 2000), with possible assistance from membrane‐associated actin polymerases, such as formins and Ena/VASP proteins (Dominguez, 2009). The fact that neither formins ...
Interstitial cells in the scars of human myocardial infarctions of different postinfarction times (6 hours to 17 years old) were characterized by antibodies to alpha-smooth muscle actin (ASMA), vimentin, and desmin. Basal lamina deposition was studied with antibodies to the basal lamina protein type …
Anti-Actin Antibody, Alexa Fluor 488 Conjugate clone, from rabbit, ALEXA FLUOR® 488; Synonym: Actin, alpha skeletal muscle, Alpha-actin-1; find Sigma-Aldrich-ABT1485-AF488 MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich.
Anti-Actin Antibody, clone C4 ascites fluid, clone C4, Chemicon®; Synonym: MAB1501X, MAB1501R; find Sigma-Aldrich-MAB1501 MSDS, related peer-reviewed papers, technical documents, similar products & more at Sigma-Aldrich.
Most fungi and metazoan cells have the capacity to express multiple isoforms of Tpm, resulting from either different gene products or different post-translational modifications. The biophysical properties of each Tpm filament and the specific way in which they interact with actin can differ significantly. This cooperative interaction with the actin polymer is crucial for Tpm function because it regulates interactions with other actin-binding proteins (e.g. myosins and cofilin) (Bryce et al., 2003), as well as the biophysical and/or dynamic properties of the actin filament. Different Tpms are, therefore, able to impart distinct physical properties to different actin filaments and, thereby, dictate their function. As many cell types can express multiple Tpm isoforms, it is crucial for the viability, function and mobility of a cell to recruit the appropriate Tpm to an actin polymer at the correct place and time (Bach et al., 2009). Indeed, we know that different Tpms are sorted to different actin ...
Work in T cells has demonstrated that actin cytoskeleton rearrangement and lipid raft polarization induced by contact with an APC are dependent on Vav1 activity (10-12). Therefore, early signals upstream of actin polymerization that induce Vav1 phosphorylation must exist. Activation receptor 2B4 on NK cells is not likely to provide such early signals because 2B4 phosphorylation is itself dependent on actin polymerization (20). To test if LFA-1 engagement on NK cells can activate Vav1 upstream of cytoskeleton rearrangements, actin polymerization was blocked by treatment with cytochalasin D and Latrunculin A. As shown in Fig. 3 B, these inhibitors did not block the Vav1 phosphorylation induced by SC2-ICAM cells. In contrast, and consistent with the actin polymerization-dependent phosphorylation of 2B4 (20), the enhancement of Vav1 phosphorylation due to coengagement of 2B4 with LFA-1 was blocked by cytochalasin D and Latrunculin A (Fig. 3 B). These results show that these inhibitors were effective ...
TY - JOUR. T1 - Formins. T2 - Processive cappers of growing actin filaments. AU - Watanabe, Naoki. AU - Higashida, Chiharu. PY - 2004/11/15. Y1 - 2004/11/15. N2 - Taking the advantage of single-molecule imaging, our recent study has revealed surprisingly long processive movement of a Formin protein, mDia1, surfing along with the growing end of actin filaments in living cells. This finding provides direct evidence for the ability of Formins to function as processive cappers that has been postulated from several lines of evidence in biochemical studies. With nucleating filaments from the profilin-actin pool, Formins may effectively generate long actin filaments, and contribute to the generation of the specific actin-based structures, that is, the contractile ring in cytokinesis, actin stress fibers in animal cells, and yeast actin cables. Furthermore, Formins have the potential to function as actin polymerization-driven molecular motors. Although much remains to be tested about the role of this ...
Tropomyosin (Tpm) isoforms are the master regulators of the functions of individual actin filaments in fungi and metazoans. Tpms are coiled-coil parallel dimers that form a head-to-tail polymer along the length of actin filaments. Yeast only has two Tpm isoforms, whereas mammals have over 40. Each cytoskeletal actin filament contains a homopolymer of Tpm homodimers, resulting in a filament of uniform Tpm composition along its length. Evidence for this master regulator role is based on four core sets of observation. First, spatially and functionally distinct actin filaments contain different Tpm isoforms, and recent data suggest that members of the formin family of actin filament nucleators can specify which Tpm isoform is added to the growing actin filament. Second, Tpms regulate whole-organism physiology in terms of morphogenesis, cell proliferation, vesicle trafficking, biomechanics, glucose metabolism and organ size in an isoform-specific manner. Third, Tpms achieve these functional outputs ...
TY - JOUR. T1 - Actin mRNA localizes in the absence of protein synthesis. AU - Sundell, C. L.. AU - Singer, R. H.. PY - 1990. Y1 - 1990. N2 - Actin mRNA is localized in chicken embryo fibroblasts to the distal regions of leading lamellae, but not within the ruffling edges. In this investigation we have addressed the role of actin translation in this process. The translocation of actin mRNA to the cell periphery was studied by monitoring the distribution of actin mRNA in cells during spreading. Within 90 min, actin mRNA moved from a perinuclear to a peripheral distribution. Formation of lamellipodia preceded actin mRNA localization, indicating that localization is not a prerequisite for this event. Neither puromycin (which dissociates ribosomes from mRNA) nor cycloheximide (which stabilizes ribosomes on mRNA) had any effect on this movement of actin mRNA. Anchoring of actin mRNA was studied using cells with peripherally localized actin mRNA. No change in actin mRNA localization was observed for ...
Intestinal epithelial barrier is critical for the maintenance of normal gut homeostasis and disruption of this barrier may trigger or exaggerate mucosal inflammation. The actin cytoskeleton is a key regulator of barrier structure and function, controlling the assembly and permeability of epithelial adherens and tight junctions. Epithelial cells express two actin isoforms: a β-cytoplasmic actin and γ-cytoplasmic actin. Our previous in vitro studies demonstrated that these actin isoforms play distinctive roles in establishing the intestinal epithelial barrier, by controlling the organization of different junctional complexes. It remains unknown, whether β-actin and γ-actin have unique or redundant functions in regulating the gut barrier in vivo. To address this question, we selectively knocked out β-actin expression in mouse intestinal epithelium. Mice with intestinal epithelial knockout of β-actin do not display gastrointestinal abnormalities or gross alterations of colonic mucosal architecture.
Cell migration involves a coordinated cycle of plasma membrane protrusion at the leading edge, adhesion site formation under the protrusion, disruption of older adhesion sites at the cell rear, and cytoskeleton contraction against adhesions to yield cell body movement (1). Protrusion is thought to result from actin filament (F-actin) polymerization against the plasma membrane (2), with the polymerization rate regulated by the rate of monomer addition to the fast-growing (barbed) ends of filaments. This may depend on actin-related protein 2/3 (Arp2/3) complex activation, which creates free barbed ends by branching and de novo nucleation of filaments (dendritic nucleation) (3), and on actin depolymerizing factor (ADF) cofilin, which creates free barbed ends by severing preexisting filaments and promoting depolymerization of free filament pointed ends (4). Filament growth is limited by barbed end-capping proteins and depletion of the polymerization-competent pool of actin monomers (5).. We ...
We have shown previously (Schwartz, M. A., and E. J. Luna. 1986. J. Cell Biol. 102: 2067-2075) that actin binds with positive cooperativity to plasma membranes from Dictyostelium discoideum. Actin is polymerized at the membrane surface even at concentrations well below the critical concentration for polymerization in solution. Low salt buffer that blocks actin polymerization in solution also prevents actin binding to membranes. To further explore the relationship between actin polymerization and binding to membranes, we prepared four chemically modified actins that appear to be incapable of polymerizing in solution. Three of these derivatives also lost their ability to bind to membranes. The fourth derivative (EF actin), in which histidine-40 is labeled with ethoxyformic anhydride, binds to membranes with reduced affinity. Binding curves exhibit positive cooperativity, and cross-linking experiments show that membrane-bound actin is multimeric. Thus, binding and polymerization are tightly ...
Disassembly of the epithelial apical junctional complex (AJC), composed of the tight junction (TJ) and adherens junction (AJ), is important for normal tissue remodeling and pathogen-induced disruption of epithelial barriers. Using a calcium depletion model in T84 epithelial cells, we previously found that disassembly of the AJC results in endocytosis of AJ/TJ proteins. In the present study, we investigated the role of the actin cytoskeleton in disassembly and internalization of the AJC. Calcium depletion induced reorganization of apical F-actin into contractile rings. Internalized AJ/TJ proteins colocalized with these rings. Both depolymerization and stabilization of F-actin inhibited ring formation and disassembly of the AJC, suggesting a role for actin filament turnover. Actin reorganization was accompanied by activation (dephosphorylation) of cofilin-1 and its translocation to the F-actin rings. In addition, Arp3 and cortactin colocalized with these rings. F-actin reorganization and disassembly of
Author Summary Actin is one of the best studied, evolutionary conserved and most abundant intracellular proteins. Actin can exists in globular and filamentous functionally distinct forms, and is involved in a variety of biological processes, such as muscle contraction, cell motility, cell division, vesicle and organelle movement, endocytosis, and cell signaling. Here we show a novel function of insect cytoplasmic actin, as an extracellular immune factor. Actin is externalized by insect immune competent cells upon immune challenge with bacteria or bacterial surface components, and once externalized, actin binds with high affinity to the surface of bacteria. A functional role of actins interaction with bacteria is to mediate their killing through either phagocytosis or direct antibacterial action. The globular and filamentous forms of actins appear to play distinct functions as extracellular immune factors. Actin also plays a role as a Plasmodium antagonist as it limits parasite infection of the mosquito
Quantitative and qualitative changes in cellular actin were followed during differentiation of a myeloid leukemia cell line, namely Ml, which was inducible with conditioned medium (CM). During 3 d of incubation with CM, when the Ml cells differentiated to macrophages and lost their mitotic activity, the actin content, F-actin ratio in total actin, and the actin synthesis showed an increase. A greater difference before and after differentiation was found in the ability of G-actin to polymerize. Actin harvested from CM-treated cells showed a greater ability to polymerize, depending on the increased concentration of MgCl2 and/or KCl and proteins, as compared with the actin from untreated Ml cells. Actin harvested from the Mml cell line, a macrophage line, had a particularly high polymerizability with or without CM treatment. In contrast, the actin from the D- subline, which is insensitive to CM, showed almost no polymerization. ...
Fission yeast cells use Arp2/3 complex and formin to assemble diverse filamentous actin (F-actin) networks within a common cytoplasm for endocytosis, division, and polarization. Although these homeostatic F-actin networks are usually investigated separately, competition for a limited pool of actin monomers (G-actin) helps to regulate their size and density. However, the mechanism by which G-actin is correctly distributed between rival F-actin networks is not clear. Using a combination of cell biological approaches and in vitro reconstitution of competition between actin assembly factors, we found that the small G-actin binding protein profilin directly inhibits Arp2/3 complex-mediated actin assembly. Profilin is therefore required for formin to compete effectively with excess Arp2/3 complex for limited G-actin and to assemble F-actin for contractile ring formation in dividing cells.
Cell behavior is controlled by extracellular signals that work through signal transduction pathways to regulate the organization of the actin cytoskeleton. Some of these extrinsic signals positively affect the cytoskeleton and induce actin polymerization, but extrinsic signals that negatively regulate and disassemble actin filaments also exist. A family of multidomain proteins, the MICALs, directly associates with Semaphorins, cell surface receptors involved in negative or repulsive cues. Working with purified proteins and in vivo, Hung et al. now find that actin filaments serve as a direct substrate for Micals enzymatic activity. Mical posttranslationally alters actin at its methionine 44 residue, which disrupts the association between actin monomers and cutting actin filaments. Altering the methionine 44 residue makes actin resistant to Mical-mediated disassembly in vitro and in vivo in Drosophila.. R.-J. Hung, C. W. Pak, J. R. Terman, Direct redox regulation of F-actin assembly and ...
Actin plays a major role in the structural integrity and motility of cells as well as in the intracellular dynamics of other macromolecules. Photon Correlation Spectroscopy (PCS) has been used to monitor the diffusion of polystyrene latex spheres (PLS) of different sizes within in vitro polymerized actin solutions under a variety of conditions. Specific actin-binding proteins were added to regulate the actin filament lengths as well as to cross-link filaments together. PCS measurements give information on the mobility of PLS over probing distances equal to the inverse scattering vector magnitude which range from 40 to 420 nm for the data. Results allow estimation of the mean pore sizes within the actin networks as a function of both actin concentration (0.4 - 5 mg/ml) and the presence of actin-binding proteins. Probe diffusion coefficients were measured for PLS samples in length-regulated actin networks at a fixed actin concentration, c (0.65 mg/ml) as c*, the semi-dilute overlap concentration, ...
The connection between T cell activation, plasma membrane order and actin filament dynamics was the main focus of this study. Laurdan and di-4-ANEPPDHQ, membrane order sensing probes, were shown to report only on lipid packing rather than being influenced by the presence of membrane-inserted peptides justifying their use in membrane order studies. These dyes were used to follow plasma membrane order in live cells at 37°C. Disrupting actin filaments had a disordering effect while stabilizing actin filaments had an ordering effect on the plasma membrane, indicating there is a basal level of ordered domains in resting cells. Lowering PI(4,5)P2 levels decreased the proportion of ordered domains strongly suggesting that the connection of actin filaments to the plasma membrane is responsible for the maintaining the level of ordered membrane domains. Membrane blebs, which are detached from the underlying actin filaments, contained a low fraction of ordered domains. Aggregation of membrane components ...
Actin protein derived from rabbit skeletal muscle supplied at |99% purity. Extensive list of citations and additional actin protein research tools available.
Drosophila Quail protein is required for the completion of fast cytoplasm transport from nurse cells to the oocyte, an event critical for the production of viable oocytes. The abundant network of cytoplasmic filamentous actin, established at the onset of fast transport, is absent in quail mutant egg chambers. Previously, we showed that Quail is a germline-specific protein with sequence homology to villin, a vertebrate actin-regulating protein. In this study, we combined biochemical experiments with observations in egg chambers to define more precisely the function of this protein in the regulation of actin-bundle assembly in nurse cells. We report that recombinant Quail can bind and bundle filamentous actin in vitro in a manner similar to villin at a physiological calcium concentration. In contrast to villin, Quail is unable to sever or cap filamentous actin, or to promote nucleation of new actin filaments at a high calcium concentration. Instead, Quail bundles the filaments regardless of the ...
To address the mechanism behind the altered cytoskeleton organization phenotypes of NAA80-KO cells, we analyzed the recovery rates of cytoskeletal structures in cells treated with the actin-depolymerizing drug latrunculin A (LatA). Within 60 min of LatA treatment the actin appeared to be fully depolymerized in control and NAA80-KO cells, and washout of the drug resulted in the recovery of actin filament structures, but the time of recovery was significantly delayed for NAA80-KO cells compared with control cells (Fig. S6), consistent with a direct role of actin Nt-acetylation in actin polymerization.. We next explored the in vitro effect of actin Nt-acetylation on the polymerization/depolymerization properties of actin alone or in the presence of some of the most common actin-assembly factors in cells. Cytoplasmic actin (a mixture of β and γ isoforms) was purified from control and NAA80-KO cells, and the presence or absence of Nt-acetylation was verified by Western blotting (Fig. 4A) (22). The ...
Dynamic actin network at the leading edge of the cell is linked to the extracellular matrix through focal adhesions (FAs), and at the same time it undergoes retrograde flow with different dynamics in two distinct zones: the lamellipodium (peripheral zone of fast flow), and the lamellum (zone of slow flow located between the lamellipodium and the cell body). Cell migration involves expansion of both the lamellipodium and the lamellum, as well as formation of new FAs, but it is largely unknown how the position of the boundary between the two flow zones is defined, and how FAs and actin flow mutually influence each other. We investigated dynamic relationship between focal adhesions and the boundary between the two flow zones in spreading cells. Nascent FAs first appeared in the lamellipodium. Within seconds after the formation of new FAs, the rate of actin flow decreased locally, and the lamellipodium/lamellum boundary advanced towards the new FAs. Blocking fast actin flow with cytochalasin D resulted in
To test whether the BODIPY-PtdIns(3,4,5)P3‐induced polarizing pseudopod was based on the actin cytoskeleton, cytochalasin B, an actin polymerization inhibitor, was used. When pre‐treated with cytochalasin B (5 μg ml−1) before loading with BODIPY-PtdIns(3,4,5)P3, no polarizing pseudopodia formed. After cell morphological polarization was initiated, but before full retraction of PtdIns(3,4,5)P3 into the uropod (Fig. 3C), cytochalasin B caused withdrawal of the polarizing pseudopod (Fig. 3A) without an accompanying release of BODIPY-PtdIns(3,4,5)P3, which remained immobilized and polarized (Fig. 3Af). Thus, the formation of the polarizing pseudopod was dependent on actin polymerization, but the tethering PtdIns(3,4,5)P3 was not sensitive to cytochalasin B. This latter evidence might not rule out the cytoskeleton as the immobilization tether because, unlike F‐actin in pseudopodia, the cortical actin network is largely resistant to depolymerization by cytochalasins (Sheterline et al., 1986, ...
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Background Podocyte foot process effacement accompanied by actin cytoskeleton rearrangements is a cardinal feature of many progressive human proteinuric diseases. Results By microarray profiling of mouse glomerulus, SCHIP1 emerged as one of the most highly enriched transcripts. We detected Schip1 protein in the kidney glomerulus, specifically in podocytes foot processes. Functionally, Schip1 inactivation in zebrafish by morpholino knock-down results in foot process disorganization and podocyte loss leading to proteinuria. In cultured podocytes Schip1 localizes to cortical actin-rich regions of lamellipodia, where it forms a complex with Nherf2 and ezrin, proteins known to participate in actin remodeling stimulated by PDGF beta signaling. Mechanistically, overexpression of Schip1 in vitro causes accumulation of cortical F-actin with dissolution of transversal stress fibers and promotes cell migration in response to PDGF-BB stimulation. Upon actin disassembly by latrunculin A treatment, Schip1 ...
Nuclear actin participates in many essential cellular processes including gene transcription, chromatin remodelling and mRNA processing. Actin shuttles into and out the nucleus through the action of dedicated transport receptors importin-9 and exportin-6, but how this transport is regulated remains unclear. Here, we show that RASSF1A is a novel regulator of actin nucleocytoplasmic trafficking and is required for the active maintenance of nuclear actin levels through supporting binding of exportin-6 (XPO6) to RAN GTPase. RASSF1A (Ras association domain family 1 isoform A) is a tumour suppressor gene frequently silenced by promoter hypermethylation in all major solid cancers. Specifically, we demonstrate that endogenous RASSF1A localises to the nuclear envelope (NE) and is required for nucleocytoplasmic actin transport and the concomitant regulation of myocardin-related transcription factor A (MRTF-A), a co-activator of the transcription factor serum response factor (SRF). The RASSF1A/RAN/XPO6/nuclear
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TY - JOUR. T1 - mDia1 and formins. T2 - Screw cap of the actin filament. AU - Mizuno, Hiroaki. AU - Watanabe, Naoki. N1 - Copyright: Copyright 2013 Elsevier B.V., All rights reserved.. PY - 2012. Y1 - 2012. N2 - Formin homology proteins (formins) are actin nucleation factors which remain bound to the growing barbed end and processively elongate actin filament (F-actin). Recently, we have demonstrated that a mammalian formin mDia1 rotates along the long-pitch helix of Factin during processive elongation (helical rotation) by single-molecule fluorescence polarization. We have also shown processive depolymerization of mDia1-bound Factin during which helical rotation was visualized. In the cell where F-actins are highly cross-linked, formins should rotate during filament elongation. Therefore, when formins are tightly anchored to cellular structures, formins may not elongate F-actin. Adversely, helical rotation of formins might affect the twist of F-actin. Formins could thus control actin elongation ...
Molecular probes that individually recognize the 3′ nontranslated regions of six actin genes were utilized in RNA gel blot hybridizations to detect RNAs complementary to each gene in embryonic and adult tissues of Stronglyocentrotus purpuratus. In addition the probes were used in DNA excess filter hybridizations to estimate the relative contribution of the different actin genes. All six genes produce relatively stable mRNAs, and each displays a characteristic and distinct pattern of expression. On the basis of their expression in the egg, early embryos, or in adult coelomocytes, it is concluded that genes termed CyI, CyIIa, CyIIb, CyIIIa, and CyIIIb encode cytoskeletal actin proteins. Actin gene M gives rise to mRNAs that are found only in tissues containing muscle. Actin genes CyI, CyIIa, CyIIb, and M are expressed in both adult and embryonic tissues, giving rise to transcripts 2.1-2.2 kb in length. Expression of genes CyIIIa and CyIIIb is confined to the embryo. Gene CyIIIa provides the ...
TY - JOUR. T1 - Mutants in the Dictyostelium Arp2/3 complex and chemoattractant-induced actin polymerization. AU - Langridge, Paul D.. AU - Kay, Robert R.. PY - 2007/7/15. Y1 - 2007/7/15. N2 - We have investigated the role of the Arp2/3 complex in Dictyostelium cell chemotaxis towards cyclic-AMP and in the actin polymerization that is triggered by this chemoattractant. We confirm that the Arp2/3 complex is recruited to the cell perimeter, or into a pseudopod, after cyclic-AMP stimulation and that this is coincident with actin polymerization. This recruitment is inhibited when actin polymerization is blocked using latrunculin suggesting that the complex binds to pre-existing actin filaments, rather than to a membrane associated signaling complex. We show genetically that an intact Arp2/3 complex is essential in Dictyostelium and have produced partially active mutants in two of its subunits. In these mutants both phases of actin polymerization in response to cyclic-AMP are greatly reduced. One ...
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,
TGF-β-induced antimitotic signals are highly regulated during cell proliferation under normal and pathological conditions, such as liver regeneration and cancer. Up-regulation of the transcriptional cofactors Ski and SnoN during liver regeneration may favor hepatocyte proliferation by inhibiting TGF-β signals. In this study, we found a novel mechanism that regulates Ski protein stability through TGF-β and G protein-coupled receptor (GPCR) signaling. Ski protein is distributed between the nucleus and cytoplasm of normal hepatocytes, and the molecular mechanisms controlling Ski protein stability involve the participation of actin cytoskeleton dynamics. Cytoplasmic Ski is partially associated with actin and localized in cholesterol-rich vesicles. Ski protein stability is decreased by TGF-β/Smads, GPCR/Rho signals, and actin polymerization, whereas GPCR/cAMP signals and actin depolymerization promote Ski protein stability. In conclusion, TGF-β and GPCR signals differentially regulate Ski ...
FIG 6 In vitro interaction of occidiofungin with F- and G-actin. (a) Affinity pulldown of actin using alkyne-OF. Lane 1, ladder; lane 2, 100 ng pure F-actin; lane 3, 100 ng pure G-actin; lane 4, empty; lane 5, F-actin treated with alkyne-OF; lane 6, F-actin treated with native occidiofungin; lane 7, F-actin treated with DMSO; lane 8, G-actin treated with alkyne-OF; lane 9, G-actin treated with native occidiofungin; lane 10, G-actin treated with DMSO. (b) Fluorescence microscopy of the effect of occidiofungin treatment on actin filaments visualized by fluorescently labeled phalloidin. (A) Actin filaments treated with solvent blank (DMSO). (B) Actin/native occidiofungin (24 μg actin:4 μg native occidiofungin). (C) Actin/native occidiofungin (24 μg actin:8 μg native occidiofungin). Scale bar, 5 µm. ...
Title:[Comparison of intracellular actin of thymosin alpha-1 and thymic serum factor].,Author:Deschaux P,Doublet A,Fontanges R,Journal:C R Seances Acad Sci III,1982/1/25;294(4):207-10.,Publication typ...
University of Helsinki, Faculty of Biosciences, Department of Biological and Environmental Sciences, Division of genetics and Institute of Biotechnology. The actin cytoskeleton is essential for a large variety of cell biological processes. Actin exists in either a monomeric or a filamentous form, and it is very important for many cellular functions that the local balance between these two actin populations is properly regulated. A large number of proteins participate in the regulation of actin dynamics in the cell, and twinfilin, one of the proteins examined in this thesis, belongs to this category. The second level of regulation involves proteins that crosslink or bundle actin filaments, thereby providing the cell with a certain shape. α-Actinin, the second protein studied, mainly acts as an actin crosslinking protein. Both proteins are conserved in organisms ranging from yeast to mammals. In this thesis, the roles of twinfilin and α-actinin in development were examined using Drosophila ...
The myristoylated form of c-Abl protein, as well as the P210bcr/abl protein, have been shown by indirect immunofluorescence to associate with F-actin stress fibers in fibroblasts. Analysis of deletion mutants of c-Abl stably expressed in fibroblasts maps the domain responsible for this interaction to the extreme COOH-terminus of Abl. This domain mediates the association of a heterologous protein with F-actin filaments after microinjection into NIH 3T3 cells, and directly binds to F-actin in a cosedimentation assay. Microinjection and cosedimentation assays localize the actin-binding domain to a 58 amino acid region, including a charged motif at the extreme COOH-terminus that is important for efficient binding. F-actin binding by Abl is calcium independent, and Abl competes with gelsolin for binding to F- actin. In addition to the F-actin binding domain, the COOH-terminus of Abl contains a proline-rich region that mediates binding and sequestration of G-actin, and the Abl F- and G-actin binding ...
Each myofibril consists of a large number of sarcomeres, the muscle cells smallest functional units.. Each sarcomere consists of a Z-disc in each end and an A-band in the middle. Actin filaments attached to the Z-discs and myosin filaments form the A band. It is the repetitive A-bands that give the characteristic transverse muscle strips seen under a microscope.. Actin and myosin filaments are organised so every myosin filament is surrounded by six actin filaments. The muscle contraction is a result of myosin filaments climbing on actin filaments in each sarcomere.. The actin filaments comprise of several spherical proteins in long helical chains. They consist of the proteins actin, tropomyocin and a troponin complex. All these are essential for muscle contraction.. The myosin filaments are an accumulation of approximately 300 elongated myosin molecules. Each of these proteins has a head on one end. The myosin heads function is to bind and slide on the actin filaments that lie parallel. As ...
Actin plays important roles in many biological processes, such as establishing cell polarization, accommodating protruding and retracting activities of motile cells, maintaining the physical integrity of the cell, and sensing environmental forces. All these processes are facilitated by the dynamical and mechanical properties of actin filaments, and their ability to exert or resist against forces generated in a cellular environment.. Actin filaments can assemble into a variety of architectures, including branched and crosslinked networks, parallel bundles, and anti-parallel contractile fibers. These structures provide architectural specificities for different regions of the cell, and can also organize into more complex actin-based machineries. We aim to understand how the native molecular architectures of actin-based cellular processes give rise to force generation and rigidity-sensing. We use cryo-electron tomography, and develop methodologies allowing for quantitative analysis of cellular actin ...
We describe the preparation of novel fluorescent derivatives of rabbit muscle actin and bovine tubulin, and the use of these derivatives to study the behaviour of actin filaments and microtubules in living Drosophila embryos, in which the nuclei divide at intervals of 8 to 21 min. The fluorescently labelled proteins appear to function normally in vitro and in vivo, and they allow continuous observation of the cytoskeleton in living embryos without perturbing development. By coinjecting labelled actin and tubulin into the early syncytial embryo, the spatial relationships between the distinct filament networks that they form can be followed second by second. The dynamic rearrangements of actin filaments and microtubules observed confirms and extends results obtained from previous studies, in which fixation techniques and specific staining were used to visualize the cytoskeleton in the Drosophila embryo. However, no tested fixation method produces an exact representation of the in vivo microtubule ...
Gelsolin is an actin-modulating protein that severs F-actin, caps the barbed ends of actin filaments preventing monomer exchange, and promotes the nucleation step of actin polymerisation [(PUBMED:14527663), (PUBMED:3023087)]. It can be regulated by Ca2+ and phosphoinositides [(PUBMED:3027569)]. The interaction between gelsolin and tropomyosin modulates actin dynamics [(PUBMED:23844991)]. Gelsolin also plays a role in ciliogenesis [(PUBMED:20393563)]. The structure of gelsolin has been solved [(PUBMED:9288746)]. Villin is an actin-binding protein that is found in a variety of tissues. It is able to bind to the barbed end of actin filaments with high affinity and can sever filaments [(PUBMED:3087992)]. In addition, villins activity is important for actin bundling in certain cell types [(PUBMED:2256904)]. It was first isolated as a major component of the core of intestinal microvilli [(PUBMED:287075)].. Villin/gelsolin family includes other actin-binding proteins such as severin and supervillin ...
Gelsolin is an actin-modulating protein that severs F-actin, caps the barbed ends of actin filaments preventing monomer exchange, and promotes the nucleation step of actin polymerisation [ (PUBMED:14527663) (PUBMED:3023087) ]. It can be regulated by Ca2+ and phosphoinositides [ (PUBMED:3027569) ]. The interaction between gelsolin and tropomyosin modulates actin dynamics [ (PUBMED:23844991) ]. Gelsolin also plays a role in ciliogenesis [ (PUBMED:20393563) ]. The structure of gelsolin has been solved [ (PUBMED:9288746) ]. Villin is an actin-binding protein that is found in a variety of tissues. It is able to bind to the barbed end of actin filaments with high affinity and can sever filaments [ (PUBMED:3087992) ]. In addition, villins activity is important for actin bundling in certain cell types [ (PUBMED:2256904) ]. It was first isolated as a major component of the core of intestinal microvilli [ (PUBMED:287075) ]. Villin/gelsolin family includes other actin-binding proteins such as severin and ...
In striated muscle the actin cytoskeleton is differentiated into myofibrils. or Axitinib muscles diseases. Therefore proper regulation of actin dynamics in striated muscle is crucial for maintenance and assembly of functional myofibrils. Recent studies have got recommended that both enhancers of actin dynamics and stabilizers of actin filaments are essential for sarcomeric actin company. Further investigation from the regulatory system of actin dynamics in striated muscles should be an integral to focusing on how myofibrils develop and work. ? 2010 Wiley-Liss Inc. continues to be used being a model to review set up and function of cross-striated myofibrils [Fyrberg and Beall 1990 Many invertebrates including nematodes annelids and molluscs possess obliquely striated muscles where sarcomeres are aligned obliquely towards the Z-band-like buildings [Rosenbluth 1965 Your body wall structure muscles from the nematode is normally a consultant example and continues to be thoroughly studied using ...
TY - JOUR. T1 - Competition for actin between two distinct F-actin networks defines a bistable switch for cell polarization. AU - Lomakin, Alexis J.. AU - Lee, Kun Chun. AU - Han, Sangyoon J.. AU - Bui, Duyen A.. AU - Davidson, Michael. AU - Mogilner, Alex. AU - Danuser, Gaudenz. PY - 2015/11/1. Y1 - 2015/11/1. N2 - Symmetry-breaking polarization enables functional plasticity of cells and tissues and is yet not well understood. Here we show that epithelial cells, hard-wired to maintain a static morphology and to preserve tissue organization, can spontaneously switch to a migratory polarized phenotype after relaxation of the actomyosin cytoskeleton. We find that myosin II engages actin in the formation of cortical actomyosin bundles and thus makes it unavailable for deployment in the process of dendritic growth normally driving cell motility. Under low-contractility regimes, epithelial cells polarize in a front-back manner owing to the emergence of actin retrograde flows powered by dendritic ...
TY - JOUR. T1 - Evidence That Actin Depolymerization Protects Hippocampal Neurons against Excitotoxicity by Stabilizing [Ca2+]i. AU - Furukawa, Katsutoshi. AU - Smith-Swintosky, Virginia L.. AU - Mattson, Mark P.. PY - 1995/6. Y1 - 1995/6. N2 - Calcium influx through glutamate receptors and voltage-dependent channels mediates an array of functional and structural responses in neurons. However, unrestrained Ca2+ influx can injure and kill neurons; a mechanism implicated in both acute and chronic neurodegenerative disorders. Data reported here indicate that depolymerization of actin filaments can stabilize intracellular free calcium levels ([Ca2+]i) and protect hippocampal neurons against excitotoxic injury. Studies with fluorescein-labeled phalloidin showed that cytochalasin D and glutamate each induced actin filament depolymerization. The microfilament-disrupting agent cytochalasin D protected cultured rat hippocampal neurons against glutamate toxicity, whereas the actin filament-stabilizing ...
The ,italic,ampA,/italic, gene encodes a secreted protein that modulates cell adhesion, actin polymerization, endocytosis, and cell migration. AmpA is secreted into the supernatant during development, and remains cell associated during growth. AmpA loss in growing cells results in an increase in cell adhesion, and a reduction in F actin. Over expression of AmpA reduces adhesion and increases F actin. As a result of these changes in the cytoskeleton and in adhesion, I have shown AmpA influences cell migration. AmpA knockout cells are defective in migration on top of agar compared to wild type. AmpA over expressing cells migrate better than wild type on top of agar. This defect in the knockout can be rescued by placing the cells in a 3D environment where they migrate under agar. Knockout cells migrate better than wild type under these conditions and over expressing cells migrate about the same as wild type. In order to visualize actin dynamics in live cells, wild type, AmpA KO and AmpA ...
CiteSeerX - Scientific documents that cite the following paper: Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family Gtpases,
The C-type lectin-like receptor 2 (CLEC-2)activates platelets through Src and Syk tyrosine kinases via a single cytoplasmic YxxL motif known as a hem immunoreceptor tyrosine-based activation motif (hemITAM).Here, we demonstrate using sucrose gradient ultracentrifugation and methyl--cyclodextrin treatment that CLEC-2 translocates to lipid rafts upon ligand engagement and that translocation is essential for hemITAM phosphorylation and signal initiation. HemITAM phosphorylation, but not translocation, is also critically dependent on actin polymerization,Rac1 activation, and release of ADP and thromboxane A2 (TxA2). The role of ADP and TxA2 in mediating hosphorylation is dependent on ligand engagement and rac activation but is independent of platelet aggregation. In contrast,tyrosine phosphorylation of the GPVIFcR -chain ITAM, which has 2 YxxL motifs,is independent of actin polymerization and secondary mediators. These results reveal a unique series of proximal events in CLEC-2 phosphorylation ...
In chronic active hepatitis, very strong alpha-SMA staining was detected at the site of piecemeal necrosis and adjacent lobules. A-SMA expression was decreased in some cases after interferon treatment. In cases of transplanted liver biopsies, expression of intralobular alpha-SMA was diffusely increased but showed no correlation with degree of acute rejection. Cirrhotic livers revealed strong alpha-SMA positivity in fibrous septae as well as in the perisinusoidal space of intact hepatocytes at the leading edge of fibrosis. Interlobular bile ducts were concentrically circumscribed by alpha-SMA positive cells in cases of intrahepatic cholelithiasis. In trabecular type hepatocellular carcinomas, most sinusoidal lining cells were positive for alpha-SMA. Most intralobular alpha-SMA positive cells represent, if not all, perisinusoidal cells (PSCs) which are involved in intralobular fibrogenesis in various liver diseases. PMID: 8305144. ...
Purpose: : PAAs are temporary polygonal, hub and spoke arrangements of actin seen in the first few hours of tissue culture while the cells are settling but then are lost. CLANs are also hub and spoke arrangements of actin that are slowly induced in confluent cultures by steroids, TGFbeta and others and persist. We wished to determine whether or not CLANs and PAAs are one in the same thing so that rapidly forming PAAs can legitimately be used as a model for the slower forming CLANs that we know to form in vivo and are associated with glaucoma in a way that is poorly understood. Methods: : We stain actin in TM cells both in vitro and in situ using phalloid-FITC and image cells either with conventional immunofluorescence or by confocal microscopy. We have a large collection of PAAs and CLANs images and from these over 50 images were selected and handed over in a masked fashion to our reading team who used Image J Software (NIH) to measure CLAN and PAA territories, height, circularity, incidence of ...
Manié S, Schmid-Alliana A, Kubar J, Ferrua B, Rossi B 1993 Disruption of microtubule network in human monocytes induces expression of interleukin-1 but not that of interleukin-6 nor tumor necrosis factor-α: Involvement of protein kinase a stimulation J Biol Chem 268:13675-13681 ...
The studies presented here clearly demonstrated that TGF-β1 triggers the nuclear translocation of MRTFs, which activates the two parallel pathways during EMT (Fig. 10 J). One pathway up-regulates the expression of EMT-regulating genes, such as slug, via MRTFs, Smad3, and GCCG-like motifs, leading to dissociation of cell-cell contacts. The other up-regulates the expression of actin cytoskeletal genes via MRTFs, SRF, and CArG box, resulting in remodeling of the actin cytoskeleton.. Recent studies demonstrate that MRTFs associate with monomeric G-actin through their RPEL motifs, which anchor MRTFs in the cytoplasm (Miralles et al., 2003; Posern et al., 2004). Activated Rho reduces the cytoplasmic G-actin pool by enhancing actin polymerization, and then triggers the dissociation of MRTFs from G-actin, resulting in the nuclear translocation of MRTFs. TGF-β1 stimulation enhances the Rho activity in many kinds of epithelial cell lines (Bhowmick et al., 2001, 2003; Tian et al., 2003). We demonstrated ...
Abbkine Scientific Co. Ltd is known for making quality life science products and tools and it recently announced the official launch of its new antibody - the Anti-Plant Actin Mouse Monoclonal Antibody (3T3).. The antibody otherwise known as AT3G12110 antibody is a Plant Actin Antibody, which is an essential component of cell cytoskeleton. The substance also plays a critical role in the streaming of cytoplasmic, determination of cell shape, cell division and extension growth.. The product is available in a liquid solution and hosted by mouse hence, Plant Actin Mouse mAb. The antibody is also a Recombinant Protein immunogen, with plant reactivity. The antibody like many of its other counterparts is affinity-purified from mouse ascites using specific immunogen by affinity-chromatography.. The Anti-Plant Actin Mouse Monoclonal Antibody (3T3) is made solely for research purpose and not intended for clinical or human use. It can also be stored for as long as one year at -20°C from date of ...
The mechanical properties of a cell are defined mainly by the cytoskeleton. One contributor within this three-dimensional structure is the actin cortex which is located underneath the lipid bilayer. It forms a nearly isotropic and densely cross-linked protein network. We present a continuum mechanical formulation for describing the mechanical properties of in vitro model systems based on their micro-structure, i.e. the behavior of a single filament and its spatial arrangement. The network is considered elastic, viscous effects being neglected. Filamentous actin is a biopolymer with a highly nonlinear force-stretch relationship. This can be well described by a worm-like chain model that includes extensibility of the filament, which we call the . β-model. A comparison with experimental data shows good agreement with values for the physically interpretable parameters. To make these properties applicable to three dimensions we used a non-affine micro-sphere network, which accounts for filaments, ...
p,Giardia intestinalis, a human intestinal parasite and member of what is perhaps the earliest-diverging eukaryotic lineage, contains the most divergent eukaryotic actin identified to date and is the first eukaryote known to lack all canonical actin-binding proteins (ABPs). We sought to investigate the properties and functions of the actin cytoskeleton in Giardia to determine whether Giardia actin (giActin) has reduced or conserved roles in core cellular processes. In vitro polymerization of giActin produced filaments, indicating that this divergent actin is a true filament-forming actin. We generated an anti-giActin antibody to localize giActin throughout the cell cycle. GiActin localized to the cortex, nuclei, internal axonemes, and formed C-shaped filaments along the anterior of the cell and a flagella-bundling helix. These structures were regulated with the cell cycle and in encysting cells giActin was recruited to the Golgi-like cyst wall processing vesicles. Knockdown of giActin ...
The Corynebacterium glutamicum ATCC 13032 prophage CGP3 encodes an actin-like protein, AlpC that was shown to be involved in viral DNA transport and efficient viral DNA replication. AlpC binds to an adapter, AlpA that in turn binds to specific DNA sequences, termed alpS sites. Thus, the AlpAC system is similar to the known plasmid segregation system ParMRS. So far it is unclear how the AlpACS system mediates DNA transport and, whether AlpA and AlpC functionally interact. We show here that AlpA modulates AlpC filamentation dynamics in a dual way. Unbound AlpA stimulates AlpC filament disassembly, while AlpA bound to alpS sites allows for AlpC filament formation. Based on these results we propose a simple search and capture model that explains DNA segregation by viral AlpACS DNA segregation system. ...
Classic pulse-chase studies have shown that actin is conveyed in slow axonal transport, but the mechanistic basis for this movement is unknown. Recently, we reported that axonal actin was surprisingly dynamic, with focal assembly/disassembly events (actin hotspots) and elongating polymers along the axon shaft (actin trails). Using a combination of live imaging, superresolution microscopy, and modeling, in this study, we explore how these dynamic structures can lead to processive transport of actin. We found relatively more actin trails elongated anterogradely as well as an overall slow, anterogradely biased flow of actin in axon shafts. Starting with first principles of monomer/filament assembly and incorporating imaging data, we generated a quantitative model simulating axonal hotspots and trails. Our simulations predict that the axonal actin dynamics indeed lead to a slow anterogradely biased flow of the population. Collectively, the data point to a surprising scenario where local assembly ...
SUMMARY, EXPLANATION AND LIMITATIONS:. Actin is an abundant cytoskeletal protein found in all cells. The proteins 42 kD peptide chain assumes two physical forms: globular actin, which may serve as a cytoplasmic storage pool, and fibrous actin, which, in conjunction with myosin, generates muscle contraction. In non-muscle cells, actin appears to be involved in a variety of functions, such as cell motility, exocytosis, and phagocytosis.. Clone: 5C5,F8,C7. Isotype: IgM. Immunogen: N-Terminal decapeptide of alpha skeletal muscle isoform of actin.. Staining pattern: Cytoplasmic.. Positive control: Tissue sample from skeletal muscle.. APPLICATIONS:. This antibody is designed for the specific localization of human Actin, Skeletal Muscle using IHC techniques in formalin-fixed, paraffin-embedded tissue sections.. ...
for the thin filaments on either side of the Z disc 8. Muscle contraction: sarcomere will shorten in length as Z discs come closer together and size of the H band decreases; the thin filaments are overlapping the thick filaments. 9. Sliding filament hypothesis: (1). Myosin heads bind ATP and split it forming ADP and Pi (2). Myosin heads bind to sites on the actin filaments (3). Myosin heads release the Pi allowing the head to bend toward the A band and Pulling the actin filaments with it; this is the power stroke (4).At end of power stroke, myosin head binds a new ATP and releases ADP; myosin head breaks away from the actin filament 10. Cross bridges: temporary union between the myosin and actin filaments 11. Troponin: protein that binds tropomyosin to actin; also is attracted to Ca+2 ions Tropomyosin: double strand of protein; blocks actin binding sites preventing myosin attachment 12. Neuromuscular junction: (1). Neuron releases acetylcholine which binds to Ach receptors on motor end Plate of ...
We have found that Ste20 or Cla4 is required to polarize the actin cytoskeleton and initiate bud emergence. Whereas mutants lacking either kinase can carry out these processes, loss of Ste20 and Cla4 blocks these events, displaying phenotypes like those of cdc42-1 mutants ( Adams et al. 1990). Because results presented here and elsewhere indicate that Cla4 and Ste20 interact and colocalize with Cdc42 at sites of polarized growth ( Adams et al. 1990; Peter et al. 1996; Benton et al. 1997; Leberer et al. 1997), these PAK homologues function as direct signaling effectors of Cdc42 in pathways that promote bud emergence and actin polarization in G1. In contrast, Ste20 and Cla4 are not required for isotropic growth or progression of the nuclear division cycle, indicating that they have primary roles in cell and actin polarization.. Several observations indicate that Ste20 and Cla4 promote bud emergence by executing functions that are at least partially distinct from those carried out by the Cdc42 ...
APPL1- and RAB5-positive signaling endosomes play a crucial role in the activation of AKT in response to extracellular stimuli. Myosin VI (MYO6) and two of its cargo adaptor proteins, GIPC and TOM1/TOM1L2, localize to these peripheral endosomes and mediate endosome association with cortical actin filaments. Loss of MYO6 leads to the displacement of these endosomes from the cell cortex and accumulation in the perinuclear space. Depletion of this myosin not only affects endosome positioning, but also induces actin and lipid remodeling consistent with endosome maturation, including accumulation of F-actin and the endosomal lipid PI(3)P. These processes acutely perturb endosome function, as both AKT phosphorylation and RAC-dependent membrane ruffling were markedly reduced by depletion of either APPL1 or MYO6. These results place MYO6 and its binding partners at a central nexus in cellular signaling linking actin dynamics at the cell surface and endosomal signaling in the cell cortex ...
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SMARCB1 (ENST00000644036.1) at chr22:23786946-23838008 - Homo sapiens SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (SMARCB1), transcript variant 1, mRNA. (from RefSeq NM_003073) SMARCB1 (ENST00000629690.2) at chr22_KI270879v1_alt:23325-70878 - Homo sapiens SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (SMARCB1), transcript variant 4, mRNA. (from RefSeq NM_001362877) SMARCB1 (ENST00000647057.1) at chr22:23786983-23834505 - SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (from HGNC SMARCB1) SMARCB1 (ENST00000646911.1) at chr22:23787258-23826248 - SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (from HGNC SMARCB1) SMARCB1 (ENST00000646723.1) at chr22:23787182-23834270 - SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily b, member 1 (from HGNC SMARCB1) SMARCB1 ...
"Is my classic movie collection covered by Florida home insurance?". Class Act Ins. January 24, 2019. "Monsieur Beaucaire". www. ...
Wieland T, Govindan VM (1974). "Phallotoxins bind to actins". FEBS Lett. 46 (1): 351-3. doi:10.1016/0014-5793(74)80404-7. PMID ...
Wieland T, Govindan VM (1974). "Phallotoxins bind to actins". FEBS Lett. 46 (1): 351-53. doi:10.1016/0014-5793(74)80404-7. PMID ...
Benjamin, Mushrooms: poisons and panaceas, p. 217 Wieland, Thomas; V.M. Govindan (1974). "Phallotoxins bind to actins". FEBS ...
"Leaving As A Class Act!". Ins&Outs. Soaps In Depth. Bauer Media Group: 13. July 15, 2013. Fairman, Michael (July 2, 2013). "The ...
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each ... Cardiac alpha actin is a 42.0 kDa protein composed of 377 amino acids. Cardiac alpha actin is a filamentous protein extending ... Actins are highly conserved proteins; the alpha actins are found in muscle tissues and are a major constituent of the ... This isoform differs from the alpha actin that is expressed in skeletal muscle, ACTA1. Alpha cardiac actin is the major protein ...
"Actin' Up , Meek Mill , Music Video". MTV Networks. Retrieved July 10, 2012. Martin, Andrew (January 17, 2013). "Video: Wale " ...
"Actin' Up , Meek Mill , Music Video". MTV Networks. Retrieved July 10, 2012. "Function Remix featuring Young Jeezy, Chris Brown ...
"Actin' Up , Meek Mill , Music Video". MTV Networks. Retrieved July 10, 2012. "Amen featuring Drake , Meek Mill , Music Video". ...
"Actin' Naturally". Amazon. Retrieved 13 November 2010. "The Big Tiger Roars Again, Pt. 2 - Benny Martin: Songs, reviews, ...
"Actin Up" 09. "Going Down!" (produced with Tre Pounds) 06. "Wuzzam, Wuzzup" 03. "Back Bone" (Young Thug) (produced with Wheezy ...
... which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is ... and expression of two novel actin genes, actin-like-7A (ACTL7A) and actin-like-7B (ACTL7B), from the familial dysautonomia ... Actin-like protein 7A is a protein that in humans is encoded by the ACTL7A gene. The protein encoded by this gene is a member ... "Entrez Gene: ACTL7A actin-like 7A". Human ACTL7A genome location and ACTL7A gene details page in the UCSC Genome Browser. ...
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... which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is ... "Entrez Gene: ACTL6B actin-like 6B". Oma Y, Nishimori K, Harata M (February 2003). "The brain-specific actin-related protein ... Actin-like protein 6B is a protein that in humans is encoded by the ACTL6B gene. The protein encoded by this gene is a member ... Harata M, Mochizuki R, Mizuno S (1999). "Two isoforms of a human actin-related protein show nuclear localization and mutually ...
Unlike the motility of actin-based cells, which is based on polar cytoskeletal elements such as actin monomers or tubulin ... In contrast to actin, MSP lacks an ATP-binding site. However, it was noticed that ATP is required for MSP filament assembly at ... The two main differences between actin and MSP is that MSP does not bind ATP and the lack of polarity in MSP, thus disabling ... Roberts TM, Stewart M (April 2000). "Acting like actin. The dynamics of the nematode major sperm protein (msp) cytoskeleton ...
"Joao Actin career". "João Carlos Barroso morre aos 69 anos; relembre a carreira do ator". ...
She investigated the regulation of actin polymerisation and how cell movement determines polarity and adhesion. She was awarded ... Jockusch, Brigitte M. (2017-01-03). The Actin Cytoskeleton. Springer. ISBN 9783319463711. Hall, Alan; Nobes, Catherine D. (1999 ... where she identified the role of the GTPase CDC42 and effectors in forming actin-rich filopodial extensions. ...
The CH domain is involved in actin binding in some members of the family. However, in calponins there is evidence that the CH ... Hartwig JH (1995). "Actin-binding proteins. 1: Spectrin super family". Protein Prof. 2 (7): 703-800. PMID 7584474. Gimona M, ... Saraste M, Castresana J (1995). "Does Vav bind to F-actin through a CH domain?". FEBS Lett. 374 (2): 149-151. doi:10.1016/0014- ... Calponin homology domain (or CH domain) is a family of actin binding domains found in both cytoskeletal proteins and signal ...
In fact, annexin A-II is itself an actin-binding protein and therefore it can form a region of interaction with actin by means ... Hayes MJ, Rescher U, Gerke V, Moss SE (August 2004). "Annexin-actin interactions". Traffic. 5 (8): 571-6. doi:10.1111/j.1600- ... in the cell membrane and facilitate actin assembly near the membrane. More recently, annexin scaffolding functions have been ... bisphosphate binding protein recruited to actin assembly sites at cellular membranes". J. Cell Sci. 117 (Pt 16): 3473-80. doi: ...
... which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is ... Actin-like protein 6A is a protein that in humans is encoded by the ACTL6A gene. This gene encodes a family member of actin- ... Together with beta-actin, it is required for maximal ATPase activity of BRG1, and for the association of the BAF complex with ... "Entrez Gene: ACTL6A actin-like 6A". Saladi SV, Ross K, Karaayvaz M, Tata PR, Mou H, Rajagopal J, Ramaswamy S, Ellisen LW (2017 ...
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"Actin Different - Belly". Retrieved 2017-07-26. Velous on Soundcloud (Articles with short description, Short ...
They contain actin. Stereocilia are found in the vas deferens, the epididymis, and the sensory cells of the inner ear. ... Like microvilli, they contain actin and lack an axoneme. This distinguishes them from cilia. They do not have a Basal body at ... Tilney, Lewis G.; Tilney, Mary S.; DeRosier, David J. (November 1992). "Actin Filaments, Stereocilia, and Hair Cells: How Cells ...
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... have found that CD-actin dimers contain ATP-bound actin upon formation. These CD-actin dimers are reduced to CD-actin monomers ... The resulting CD-actin monomer can bind ATP-actin monomer to reform the CD-actin dimer. CD is very effective; only low ... In contrast, latrunculin inhibits actin filament polymerization by binding to actin monomers. Actin microfilaments have been ... Once bound, cytochalasins essentially cap the end of the new actin filament. One cytochalasin will bind to one actin filament. ...
Spiro, J.D. (August 26, 1956). "Milwaukee's Actin' Tom Laughlin". Milwaukee Journal. Retrieved February 19, 2010. "Stock Group ...
Arnold, Chuck (February 1, 1994). "She's Just Actin' Jackson". Archived from the original on March 3, 2016. ...
Actin took a slight lead by the Black Buoy, which they extended to be several lengths up on Myosin by Hammersmith Bridge. ... 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 ... Myosin fought back before Chiswick Bridge to reduce the deficit, but Actin won by around two lengths. Oxford's men's trial race ...
Lee E, De Camilli P (2002). "Dynamin at actin tails". Proc. Natl. Acad. Sci. U.S.A. 99 (1): 161-6. doi:10.1073/pnas.012607799. ... Orth JD, McNiven MA (2003). "Dynamin at the actin-membrane interface". Curr. Opin. Cell Biol. 15 (1): 31-9. doi:10.1016/S0955- ... Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that ... 2003). "Dynamin2 and cortactin regulate actin assembly and filament organization". Curr. Biol. 12 (21): 1852-7. doi:10.1016/ ...
... Retrieved 2019-10-22. Bugyi, Beáta; Kellermayer, Miklós (2019-05-15). "The discovery of actin: 'to see what ... Straub was able to isolate the actin and he, Banga, and other members of the lab carried out extensive characterization of ... Further work by another lab member, Brunó Straub, showed that Banga had extracted a combination of actin and myosin, which they ... Ilona Banga (1906-1998) was a Hungarian biochemist known for co-discovering actomyosin and working to characterize how actin ...
Actin-accumulation myopathy is a disorder that primarily affects skeletal muscles, which are muscles that the body uses for ... ACTA1 gene mutations that cause actin-accumulation myopathy may affect the way the skeletal α-actin protein binds to ATP. ATP ... This gene provides instructions for making a protein called skeletal alpha (α)-actin, which is a member of the actin protein ... Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. Nat Genet. 1999 Oct;23 ...
Apart from that striking feature, patches of F-actin and deep actin filament bundles have been described along the lengths of ... Apart from that striking feature, patches of F-actin and deep actin filament bundles have been described along the lengths of ... In this review, we focus on recent developments regarding the role of actin in dendrite morphology, the regulation of actin ... In this review, we focus on recent developments regarding the role of actin in dendrite morphology, the regulation of actin ...
We have modeled the polymerization of these filaments based upon the interactions of globular actin through a probabilistic ... we have developed a computational technique that is able to probe the self-assembly of actin filaments through a lattice based ... Understanding Actin Organization in Cell Structure through Lattice Based Monte Carlo Simulations. Kathleen Puskar1, Leonard ... We have modeled the polymerization of these filaments based upon the interactions of globular actin through a probabilistic ...
Cucurbitacin I results in accumulation of actin filaments in cells by a unique indirect mechanism. Furthermore, the proximal ... In in vitro actin depolymerization experiments, cucurbitacin I had no effect on the rate of actin filament disassembly at the ... Therefore, cucurbitacin I targets some factor involved in cellular actin dynamics other than actin itself. Two candidate ... Cucurbitacin I inhibits cell motility by indirectly interfering with actin dynamics PLoS One. 2010 Nov 24;5(11):e14039. doi: ...
alpha-smooth muscle actin, mouse. Known as: alpha-SMA, mouse, alphaSMA, mouse ...
MUbio Anti-actin beta-cytoplasmic Monoclonal (4C2), Catalog # MUB0110P. Tested in Western Blot (WB), Immunohistochemistry ( ...
Actin is the main component of thin muscle filaments. It is found in two forms: monomeric G-actin (globular actin) and F-actin ... filamentous actin), which results from the polymerization of G-actin to a helix made of two strands. Interaction of the actin ... In nonmuscle cells, some of the actin is polymerized into microfilaments and is an important component of the cytoskeleton. ... actinZoomA-Z. Subject - Biochemistry, Cell Biology. ...
Beta-actin is commonly used as a western blot loading control as is expressed within all eukaryotic cell types and is not ... The two most commonly used controls are beta-actin and Glyceraldehyde 3-phosphate dehydrogenase (GADPH). Beta-actin is commonly ... Beta-actin and GADPH as controls. The control protein used in western blotting must be present across all cell types or tissue ... Beta-actin is approximately 42 kDa and GADPH is approximately 36 kDa. They are used as a control as they remain stable in the ...
New on bioRxiv: Our paper on Furrowing without F-actin * By Masayuki Onishi ... Cleavage-furrow formation without F-actin in Chlamydomonas Masayuki Onishi, James G Umen, Frederick R Cross, John R Pringle ...
Actin Images*Actin Interacting Proteins That Can Be Studied By Two-Hybrid ... Aip1p Accelerates Actin Filament Disassembly in a Cofilin Dependant Manner. *Cofilin Mis-localizes in Strains Lacking Aip1p or ... Aip1p Accelerates Actin Filament Disassembly in a Cofilin Dependant Manner. *Cofilin Mis-localizes in Strains Lacking Aip1p or ... Aip1p Localization to the Cortical Patch Requires the Aip1p-Actin Interaction. *Substoichiometric Amounts of Aip1p Accelerate ...
beta Actin 29 results for beta Actin Sort by. Relevance. Customer reviews. Number of references. Recently added. Alphabetical ... HRP Anti-beta Actin antibody [mAbcam 8226] - Loading Control (ab20272) Reviews (17) Specific References (235) ... HRP Anti-beta Actin antibody [mAbcam 8224] - Loading Control (ab197277) Reviews (1) Specific References (8) ... Anti-beta Actin antibody [mAbcam 8226] - Loading Control (ab8226) Reviews (136) Specific References (2336) ...
Prachee Avasthi, assistant professor of cell biology, and her team have published four scholarly articles on actin protein and ... 2: Actin.. In addition to microtubules, an alga cells skeleton also contains actin. Actin proteins join end to end in a strand ... This mutant in the second, lesser-known actin helped to prove that actin in these algae was more important than researchers ... Scientists knew that this type of algae had two types of actin, but they knew little about what it did in the cell. Then came ...
All injected actin was associated with DBP, without evidence of free actin, actin-gelsolin complexes or actin oligomers. Tissue ... We examined the plasma disappearance and tissue appearance of 125I-DBP, 125I-G-actin, and the DBP-G-actin complex after their ... After 125I-G-actin (nanomole) injection, plasma disappearance paralleled that of DBP and DBP-actin. ... Although more complex phenomena (plasma entry of F-actin and intracellular actin binding proteins) would occur in vivo after ...
"β-actin-luc Random Transgenic emerging mouse model from the Taconic Biosciences. Find your model and order today. ... β-actin-luc tissue expression survey from 2 male and 2 female mice (Fig. 1A). Data are expressed in Relative Light Units (RLU)/ ... The β-actin-luc mouse was developed by Caliper Life Sciences. The model was created by microinjecting a transgene containing a ... Carries a 14 kb fragment of the murine β-actin promoter isolated from genomic DNA, a chimeric intron and modified firefly ...
Shop Siemens Healthineers Dade Actin™ FSL ... Dade Actin™ FSL Activated PTT reagent exhibits increased ...
View mouse Actr6 Chr10:89547833-89568157 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
At low concentrations, this protein increased the low shear viscosity to greater than that of the actin control, whereas higher ... Brown, Susan S. (1985)."A Ca 2+ insensitive actin-crosslinking protein from Dicytostelium discoideum." Cell Motility and the ... This protein resembled a previously reported actin-binding protein from Dictyostelium [Fechheimer and Taylor, 84, J Biol Chem ... A Ca 2+ insensitive actin-crosslinking protein from Dicytostelium discoideum. Brown, Susan S. ...
Primer Set for studying beta-Actin in the research area. ... SimpleChIP® Human β-Actin 3 UTR Primers SimpleChIP® Human β- ... SimpleChIP® Human β-Actin 3 UTR Primers 13669. Toggle Between Dark and Light Modes Filter: *ChIP ... The β-actin gene is actively transcribed in all cell types and its promoter is highly enriched for histone modifications ... SimpleChIP® Human β-Actin 3 UTR Primers contain a mix of forward and reverse PCR primers that are specific to the human β- ...
An investigation of defective actin turnover during cytokinesis shows that robust rearrangement of actin is crucial for proper ... Actin turnover maintains actin filament homeostasis during cytokinetic ring contraction. J Cell Biol 216, 2657-2667. Crossref, ... actin turnover was perturbed by using RNAi to target proteins involved in actin turnover, and injecting embryos with drugs that ... Movement of actin and myosin clusters around the S. pombe AMR has been observed previously in WT cells (Wollrab et al., 2016); ...
... beta actin antibody for ICC/IF, WB, and IHC-P. These new products are only for research use, and are not intended... ... The anti beta actin monoclonal antibodies can be used to detect beta-actin, which is one of six different actin proteins. ... Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all ... Beta actin antibodies are highly complementary to our existing antibody offerings and will further help us meet the continuing ...
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Cell migration is heavily interconnected with plasma membrane protrusion and retraction (collectively termed
Neuroscience research articles are provided.. What is neuroscience? Neuroscience is the scientific study of nervous systems. Neuroscience can involve research from many branches of science including those involving neurology, brain science, neurobiology, psychology, computer science, artificial intelligence, statistics, prosthetics, neuroimaging, engineering, medicine, physics, mathematics, pharmacology, electrophysiology, biology, robotics and technology. ...
In total cytosolic actin protein pool, some are found as part of the actin filaments (known as F-actin), and the remaining is ... G-actin polymerizes noncovalently into actin filaments, called F-actin.. Which cytoskeletal filaments are found in a lattice ... Where is the actin filament located?. author. 2022-09-29. Where is the actin filament located?. In many types of cells, ... Where is actin found in the sarcomere?. The actin filaments are attached at their plus ends to the Z disc, which includes the ...
Reacts with the a-smooth muscle isoform of actin, and with smooth muscle cells of blood vessels and parenchymal ... Acetyl group and the four amino acids on the terminal end of the peptide chain of alpha-smoooth muscle actin.. Presentation:. ... Alpha-smooth muscle actin, a differentiation marker of smooth muscle cells, is present in microfilamentous bundles of pericytes ... 6. Schmitt-Gräff A, Krüger S, Bochard F, Gabbiani G, Denk H. Modulation of alpha smooth muscle actin and desmin expression in ...
Casey Veggies - "Actin Up" f. Dom Kennedy (prod. DJ Mustard). blame it on Meka September 18, 2015 ... Casey Veggies - "Actin Up" f. Dom Kennedy (prod. DJ Mustard) was last modified: March 31st, 2018 by Meka ...
Abl kinases are known to organize actin rearrangement both directly, via binding domains for G-actin and F-actin, and ... F-actin staining is weak because of competitive binding of jasplakinolide and phalloidin to F-actin. Note that F-actin staining ... This suggests that Abl activity leads to actin destabilization, which induces dendrite formation. The actin depolymerization ... Regulation of the actin cytoskeleton during dendrogenesis by Abl family kinases. The Abl family kinases are involved in the ...
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Learn more about Actin Stress Fibers and Focal Adhesions During EMT including related products, articles and interactive ... Actin stress fiber assembly is regulated by Rho family GTPases, and fiber stability is maintained by inhibition of Actin ... Actin is assembled into contractile stress fibers, which are organized structures consisting of parallel Actin fibers with ... Actin Stress Fibers and Focal Adhesions During EMT. View Epithelial to. Mesenchymal Transition. Wall Poster. ...
... with both signaling cascades relying on the dynamic nature of the microtubule and F-actin cytoskeleton which is essential for ... actin and actin binding proteins (ABPs). ABPs dynamically organize F-actin into many different structural forms such as ... 1). Understanding the actin cytoskeletons role in mechanotransduction goes beyond the basic biology underlying force-induced ... A primary means by which F-actin transduces these signals is through its connections to focal adhesions and adherens junctions ...
  • Actin proteins are important for cell movement and the tensing of muscle fibers (muscle contraction). (
  • We have modeled the polymerization of these filaments based upon the interactions of globular actin through a probabilistic model encompassing both inert and active proteins. (
  • Two candidate proteins that play roles in actin depolymerization are the actin-severing proteins cofilin and gelsolin. (
  • Recent studies have discovered that housekeeping proteins, such as GADPH and beta-actin, may be altered by the experimental conditions and skew the results. (
  • Although more complex phenomena (plasma entry of F-actin and intracellular actin binding proteins) would occur in vivo after cell lysis, our results suggest a role for DBP in the sequestration and disposition of actin monomers in the circulation. (
  • Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. (
  • The anti beta actin monoclonal antibodies can be used to detect beta-actin, which is one of six different actin proteins. (
  • In many types of cells, networks of actin filaments are found beneath the cell cortex, which is the meshwork of membrane-associated proteins that supports and strengthens the plasma membrane. (
  • Which proteins are actin filaments? (
  • During mitosis, intracellular organelles are transported by motor proteins to the daughter cells along actin cables. (
  • In muscle cells, actin filaments are aligned and myosin proteins generate forces on the filaments to support muscle contraction. (
  • Myofibroblasts from diverse pathologic settings are heterogenous in their content of actin isoforms and intermediate filament proteins. (
  • Specifically, Actin is assembled into contractile stress fibers, which are organized structures consisting of parallel Actin fibers with periodic cross-linking proteins such as alpha-Actinin and Myosin II motor proteins. (
  • F-) actin and actin binding proteins (ABPs). (
  • People with faulty actin proteins often suffer from muscle disease. (
  • Using an in vitro approach, we studied the effect of the IQGAP protein fragment Rng2(1-189) on the geometry of actin filaments when tethered to supported lipid bilayers all reconstituted from purified proteins. (
  • After 10 min of incubation, His 6 -Curly or other variants of histidine-tagged actin binding proteins at a final concentration of 10 nM were added and a short time after (1 - 5 min) binding of actin to the SLB could be observed using TIRF microscopy. (
  • In this study, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by the binding of proteins to the lateral filament surface. (
  • these proteins activate the Arp2/3 complex to nucleate new actin filaments. (
  • The importance of WASP proteins was immediately recognised when it became clear that they were involved in linking signalling events to the regulation of the actin cytoskeleton. (
  • In particular, SiR-Actin and SiR-Tubulin are the only stains available on the market which enable live cell imaging of the major cytoskeletal cellular structures - without the need to transfect cells with vectors carrying the information for fluorescently labeled tubulin or actin or related binding proteins. (
  • The WH2 (Wiscott - Aldridge syndrome protein homology domain 2) repeat is an actin interacting motif found in monomer sequestering and filament assembly proteins. (
  • The structure implies that multiple WH2 motif-containing proteins will associate longitudinally with actin filaments. (
  • In view of the fact that the signaling pathway of PI3-kinase controls microfilaments and translocation of actin-associated proteins, the current study was designed to investigate the PI3-kinase-mediated nuclear translocation of Nrf2 and the interaction of Nrf2 with actin. (
  • RPEL1 and RPEL2 of MC bind actin weakly compared with those of MAL, while RPEL3 is of comparable and low affinity in the two proteins. (
  • Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). (
  • A number of actin-binding proteins, including spectrin, alpha-actinin and fimbrin, contain a 250 amino acid stretch called the actin binding domain (ABD). (
  • In addition, the CH domain occurs also in a number of proteins not known to bind actin, a notable example being the vav protooncogene. (
  • Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. (
  • While it is known that this versatility is the result of the many actin-remodeling activities of actin-binding proteins, such as Arp2/3 and cofilin, recent work also implicates posttranslational acetylation or arginylation of the actin N terminus itself as an equally important regulatory mechanism. (
  • Myofibrils are composed of long proteins including actin, myosin, and titin, and other proteins that hold them together. (
  • Actin filaments are attached to Z- bands which are composed of actinin and other proteins. (
  • Chemotaxis of neutrophils involves movement of pseudopodia and polymerization of cytoskeletal proteins or actin. (
  • The name actin-accumulation myopathy derives from characteristic accumulations in muscle cells of filaments composed of a protein called actin . (
  • This gene provides instructions for making a protein called skeletal alpha (α)-actin, which is a member of the actin protein family found in skeletal muscles. (
  • ACTA1 gene mutations that cause actin-accumulation myopathy may affect the way the skeletal α-actin protein binds to ATP. (
  • Actin is a versatile and ubiquitous cytoskeletal protein that plays a major role in both the establishment and the maintenance of neuronal polarity. (
  • In this review, we focus on recent developments regarding the role of actin in dendrite morphology, the regulation of actin dynamics by internal and external factors, and the role of F-actin in dendritic protein trafficking. (
  • Dr. Prachee Avasthi, assistant professor of cell biology, and her team have published four scholarly articles on actin protein and how it affects cell cilia. (
  • Vitamin D binding protein sequesters monomeric actin in the circulation of the rat. (
  • Plasma vitamin D binding protein (DBP) may scavenge actin released during cell lysis. (
  • We have isolated a 30,000-dalton protein from Dictyostelium which cosedimented with and affected the low shear viscosity of actin. (
  • At low concentrations, this protein increased the low shear viscosity to greater than that of the actin control, whereas higher concentrations decreased viscosity. (
  • This protein resembled a previously reported actin-binding protein from Dictyostelium [Fechheimer and Taylor, 84, J Biol Chem 259:4514] in electrophoretic mobility, Stokes radius, and ability to crosslink filaments, but was shown to be different by peptide mapping, lack of immunologic crossreactivity, and lack of sensitivity to calcium. (
  • By using mutants of the fission yeast actin severing protein Adf1, we observed that contracting AMRs display a "peeling" phenotype, where bundles of actin and myosin peel off from one side of the AMR, and are pulled across to the opposite side. (
  • The monomer is a globular protein called G-actin, with a molecular weight of 41,800 Da. (
  • The actin filaments are attached at their plus ends to the Z disc, which includes the crosslinking protein α-actinin. (
  • Actin is a very abundant protein in the cytosol, about 10 % of the total cytosolic protein content. (
  • In total cytosolic actin protein pool, some are found as part of the actin filaments (known as F-actin), and the remaining is free in the cytosol (known as G-actin). (
  • Nonreceptor tyrosine kinase Abl is an actin-binding protein and a key regulator of neuronal axonal development. (
  • His research group at the Netherlands Cancer Institute has once again managed to track down one of these "mystery genes" - the gene that ensures that the final form of the protein actin is created, a main component of our cell skeleton. (
  • Cell biologists are very interested in actin, because actin - a protein of which we produce more than 100 kilograms in our lifetime - is a main component of the cell skeleton and one of the most abundant molecules in a cell. (
  • Much is known about the function of actin, but how the final form of this important protein is made and which gene is behind it? (
  • We explored the relationship between regulation of the spine actin cytoskeleton, spine morphogenesis, and synapse formation by manipulating expression of the actin binding protein NrbI and its deletion mutants. (
  • This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap. (
  • Planimetric analyses of SDS-polyacrylamide gels showed the percent actin of total protein was increased by approximately 40% and the absolute amount of actin by approximately 43%, ten days after daily phalloidin treatment (50 micrograms/100 gm body weight). (
  • Neither the relative fractional rate of actin synthesis nor its synthesis as a percent of total protein synthesis was altered either at one-day or ten-day post-phalloidin treatment. (
  • Immunoblot and immunoprecipitation assays showed that the 100-kDa protein comprised both Nrf2 and actin. (
  • The extent of cortical actin disruption with various doses of either latrunculin B or Clostridium difficile toxin B (a Rho family small GTP-binding protein toxin) directly correlated with the inhibition of insulin-stimulated glucose uptake and GLUT4 translocation. (
  • In vivo time-lapse confocal fluorescent microscopy of actin-yellow fluorescent protein demonstrated that insulin stimulation initially results in cortical actin remodeling followed by an increase in polymerized actin in the peri-nuclear region. (
  • Immunoblot analysis using specific antibodies showed that the 47 kDa protein is actin. (
  • Actin, a constitutively expressed protein in higher plants, was closely related to the function such as cell division, cell movement and cell signal transduction. (
  • In the present study, actin protein was composed of 360 amino acid residues with the predicted molecular weight of 40.02 kDa and the theoretical isoelectric point of 5.85. (
  • Notably, it was concluded that actin protein might play an important role in the regulation of gene transcription in higher plants, without changeable advanced structure even if a few amino acid mutation sites. (
  • The hetero-oligomeric chaperonin of eukarya , TRiC, is required to fold the cytoskeletal protein actin . (
  • The actin filament-associated protein and Src-binding partner, AFAP-110, is an adaptor protein that links signaling molecules to actin filaments. (
  • 1. Skalli O, Ropraz P, Trzeciak A, Benzonana G, Gillesen D, Gabbiani G. A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation. (
  • Alpha-smooth muscle actin, a differentiation marker of smooth muscle cells, is present in microfilamentous bundles of pericytes. (
  • 6. Schmitt-Gräff A, Krüger S, Bochard F, Gabbiani G, Denk H. Modulation of alpha smooth muscle actin and desmin expression in perisinusoidal cells of normal and diseased human livers. (
  • Together, these studies support a critical role for Abl kinases in regulating dendrogenesis by inducing actin cytoskeletal rearrangements in cooperation with Rho GTPases. (
  • F-actin makes up the cytoskeletal element called microfilaments which measure approxiately 7nm in diameter. (
  • It is found in two forms: monomeric G-actin (globular actin) and F-actin (filamentous actin), which results from the polymerization of G-actin to a helix made of two strands. (
  • which blocks F-actin polymerization and results in AMR disintegration. (
  • Polymerization of actin filaments was induced by addition of an equal amount of 2x KMEH buffer supplemented with 2 mM Mg-ATP bringing the G-actin concentration to 5 µM. (
  • This hyperspinogenesis was accompanied by enhanced actin polymerization and spine motility. (
  • Phalloidin increases F-actin microfilament content and actin-directed immunofluorescence in hepatocytes in vivo and also increases actin polymerization and the stability of F-actin in vitro. (
  • We studied the sensitivity of immunofluorescent staining of actin to an actin depolymerizing factor (ADF) as well as actin content, degree of polymerization, and turnover in livers of in vivo phalloidin-treated rats. (
  • When the bacterium infects a mammalian host cell, ActA hijacks the host's machinery to trigger actin polymerization on the microbe's surface. (
  • As a global leading supplier of of raw materials, antibodies, and reagents for bio-technology industry, Creative Diagnostics recently expanded antibody portfolio with the launch of a series of beta actin antibody for ICC/IF, WB, and IHC-P. These new products are only for research use, and are not intended for diagnostic use. (
  • For example, Anti-ACTB monoclonal antibody (DCABH-10282), one of the products included in this release, is mouse anti-Human ACTB monoclonal antibody that can be used for ICC/IF, WB, and IHC-P. This antibody can specifically recognize beta actin in tissues or species through immunoblotting, immunofluorescence staining of cultured cell lines, and immunohistochemistry. (
  • Our mouse monoclonal antibody to beta actin is now available for global researchers, and more improved antibodies and services will be offered to meet the unmet needs of scientists working in basic research and development. (
  • Beta actin antibodies are highly complementary to our existing antibody offerings and will further help us meet the continuing demands from our customers for high quality antibodies. (
  • Pretreatment with ADF abolished anti-actin antibody (AAA) staining of normal liver but did not modify staining of livers from phalloidin-treated animals. (
  • Four stress fiber subtypes have been described based on intracellular location: ventral and dorsal stress fibers, perinuclear Actin cap, and transverse arcs. (
  • Stress fibers are specific determinants of cell mechanics [15], and cortical actin has also been reported to promote cortical rigidity [16,17]. (
  • Fig 1: 3D-SIM microscopy image of labeled Actin stress fibers in human primary dermal fibroblasts. (
  • Together, these data demonstrate that cortical actin, but not stress fibers, lamellipodia, or filopodia, plays an important regulatory role in insulin-stimulated GLUT4 translocation. (
  • F-actin and microtubules (MTs) are the main mediators of neuronal polarity. (
  • In addition to microtubules, an alga cell's skeleton also contains actin. (
  • The CA-Abl phenotype is not affected by destabilization of microtubules but is reversed partially when actin filaments are stabilized with jasplakinolide. (
  • Launched just over a year ago, SiR-Actin (Fig 1) and SiR-Tubulin (Fig 2) have been available on the market providing the most convenient tools to stain F-actin and Microtubules in living cells. (
  • The SiR dyes are coupled to binding components which specifically bind to F-actin (Jasplakinolide natural compound), Microtubules (Docetaxel), or the DNA minor groove binder bisbenzimide (Hoechst). (
  • Two interphase cells with immunofluorescence labeling of actin filaments (purple), microtubules (yellow), and nuclei (green). (
  • Rhodamine-labeled phalloidin staining of morphologically differentiated 3T3L1 adipocytes demonstrated that F-actin predominantly exists juxtaposed to and lining the inner face of the plasma membrane (cortical actin) with a smaller amount of stress fiber and/or ruffling actin confined to the cell bottom in contact with the substratum. (
  • The dissolution of the cortical actin network had no significant effect on proximal insulin receptor signaling events including insulin receptor autophosphorylation, tyrosine phosphorylation of insulin receptor substrate and Cbl, or serine/threonine phosphorylation of Akt. (
  • Importantly, the insulin stimulation of cortical actin rearrangements was completely blocked by treatment of the cells with latrunculin B, C. difficile toxin B, and jasplakinolide. (
  • Furthermore, expression of the dominant-interfering TC10/T31N mutant completely disrupted cortical actin and prevents any insulin-stimulated actin remodeling. (
  • In addition, cortical F-actin does not function in a static manner (e.g. barrier or scaffold), but insulin-stimulated dynamic cortical actin remodeling is necessary for the GLUT4 translocation process. (
  • Kanzaki, M & Pessin, JE 2001, ' Insulin-stimulated GLUT4 Translocation in Adipocytes Is Dependent upon Cortical Actin Remodeling ', Journal of Biological Chemistry , vol. 276, no. 45, pp. 42436-42444. (
  • It comprises one or two WASP homology 2 (WH2) domains, which bind to monomeric actin, followed by a short central (C) region and an acidic (A) domain, which interacts with the Arp2/3 complex. (
  • Expression of one NrbI deletion mutant, containing the actin binding domain, dramatically increased the density and length of dendritic spines with synapses. (
  • In in vitro actin depolymerization experiments, cucurbitacin I had no effect on the rate of actin filament disassembly at the nanomolar concentrations that inhibit cell migration. (
  • Actin stress fiber assembly is regulated by Rho family GTPases, and fiber stability is maintained by inhibition of Actin depolymerization. (
  • Here, we show that actin depolymerization in Arabidopsis thaliana seedlings not only triggers SA biosynthesis by ICS1, but also induces callose deposition via callose synthase PMR4. (
  • In contrast, phalloidin, an agent that prevents actin filaments from depolymerization, inhibited Nrf2 translocation and rGSTA2 induction by t -BHQ. (
  • The present study demonstrates that the PI3-kinase signaling pathway regulates rearrangement of actin microfilaments in response to oxidative stress and that depolymerization of actin causes a complex of Nrf2 bound with actin to translocate into nucleus. (
  • Apart from that striking feature, patches of F-actin and deep actin filament bundles have been described along the lengths of neurites. (
  • The viscosity decrease correlated with the formation of actin filament bundles, as seen electron microscopically. (
  • Visualizing AMR contraction face-on in adf1 -M2 and adf1 -M3 cells, we observed that bundles of myosin and (presumably) actin peeled off from one side of the AMR, and were pulled in toward the opposite side ( Figure 1A ), behavior that was not seen in wild-type (WT) cells ( Figure 1B ). (
  • More stable actin bundles remain polarized and contribute to the orientation of the microtubule network that serves as the mitotic spindle. (
  • These domains cross-link actin filaments into bundles and networks. (
  • Lo WK, Shaw AP, Paulsen DF , Mills A. Spatiotemporal distribution of zonulae adherens and associated actin bundles in both epithelium and fiber cells during chicken lens development. (
  • Therefore, cucurbitacin I targets some factor involved in cellular actin dynamics other than actin itself. (
  • Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. (
  • A central feature of actin dynamics is the capacity of filaments to polymerize and depolymerize at their ends in response to cellular conditions. (
  • Tuning elongation kinetics by exploiting the malleability of the filament structure may be a ubiquitous mechanism to generate a rich variety of cellular actin dynamics. (
  • The great diversity in actin network architectures and dynamics is exploited by cells to drive fundamental biological processes, including cell migration, endocytosis, and cell division. (
  • The structure reveals that Tbeta4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tb4 and profilin is mediated by a minor overlap in binding sites. (
  • Cultured chicken embryonic cardiomyocyte transfected with GFP control vector in the nucleus, stained with alpha-actinin at the Z-lines in red and Tropomodulin1 (at the pointed ends of the actin filame. (
  • Interaction of the actin filaments with myosin ATPase produces muscle movement. (
  • When the signal to contract is sent along a nerve to the muscle, the actin and myosin are activated. (
  • Myosin works as a motor, hydrolyzing adenosine triphosphate (ATP) to release energy in such a way that a myosin filament moves along an actin filament, causing the two filaments to slide past each other. (
  • The subsequent movement of the lever arm through its power stroke generates muscle contraction by causing myosin heads to pull on actin filaments. (
  • Muscles contract by sliding the thick (myosin) and thin (actin) filaments along each other. (
  • Myofibers contain two kinds of contractile filaments: myosin: 12-15 nm thick - 1.5 micron long, and actin: 6-7 nm thick - 1 micron long. (
  • Upon treatment of MDCK or B16-F1 cells with cucurbitacin I, there is a very rapid cessation of motility and gradual accumulation of filamentous actin aggregates. (
  • The actin cytoskeleton plays an essential role in numerous aspects of cell biology, such as cell morphology and motility. (
  • Our data support a model in which synapse formation is promoted by actin-powered motility. (
  • Using chicken embryo fibroblasts as a model system, our results indicate that the c-Yes N-terminal SH4-Unique domains are sufficient to inhibit the ability of Src527F to alter cell morphology, induce actin filament rearrangements or stimulate motility or invasive potential. (
  • We hypothesize that upon PKC activation, AFAP-110 can be cooperatively recruited to newly forming actin filaments, like those that exist in cell motility structures, and that PKC phosphorylation effects a conformational change that may enable AFAP-110 to promote actin filament cross-linking at the cell membrane. (
  • The microfilament (also called actin filament) is a helical polymer of actin sub-units, with diameter of 7 nm. (
  • This color combined image shows the spatial relationship between filamentous actin (red) and microtubule array (green) in cultured hippocampal neurons, grown for 1 day in vitro. (
  • The cellular effect of the compound is similar to that observed when cells are treated with the actin filament-stabilizing agent jasplakinolide. (
  • However, we found that, unlike jasplakinolide or phallacidin, cucurbitacin I does not directly stabilize actin filaments. (
  • Surprisingly, however, stabilization of F-actin with jasplakinolide also resulted in a dose-dependent inhibition of insulin-stimulated glucose uptake and GLUT4 translocation. (
  • Dualisotope experiments indicated that the rate of actin degradation was decreased selectively in the one- to three-day period following drug treatment. (
  • Understanding the actin cytoskeleton's role in mechanotransduction goes beyond the basic biology underlying force-induced changes in actin-based cellular structures and functions. (
  • t -BHQ relocalized Nrf2 in concert with changes in actin microfilament architecture, as visualized by superposition of immunochemically stained Nrf2 and fluorescent phalloidin-stained actin. (
  • These data indicate that c-Yes may not modulate signals associated with c-Src-induced changes in actin filament integrity and may explain why c-Yes fails to compensate for c-Src signaling in src-/- cells. (
  • Cucurbitacin I results in accumulation of actin filaments in cells by a unique indirect mechanism. (
  • Thus, phalloidin appears to stabilize actin against the depolymerizing actions of ADF, increases the proportion of F-actin without altering the size of the G-actin pool, and causes accumulation of actin by decreasing its relative rate of degradation. (
  • Beta-actin is commonly used as a western blot loading control as is expressed within all eukaryotic cell types and is not affected by cellular treatments. (
  • At the cellular level the alteration of Abl also changes actin organization consistent with RhoA inhibition. (
  • Cellular internalization appeared to be, at least in part, actin-dependent. (
  • Development of the dendritic tree is a series of dynamic events that result in the formation of a complex and highly ordered structure through abundant remodeling and reorganization of the actin and microtubule cytoskeletons. (
  • This effect is actin independent, but microtubule dependent. (
  • With the development of super-resolution microscopy in the past few years, previously unknown structures of the actin cytoskeleton have been uncovered: a periodic lattice consisting of actin and spectrin seems to pervade not only the whole axon, but also dendrites and even the necks of dendritic spines. (
  • Perhaps the most striking F-actin-based structures in dendrites are so-called spines, small membranous protrusions that harbor synapses. (
  • Actin-based motile structures are disassembled before cell division, which causes the cell to stop moving and become more rounded. (
  • Especially we aimed at clarifying the regulatory mechanisms of sub-membrane actin structures in these cells by activation of actomyosin formation using calyculin A. This technique revealed that TIG-1 and Hela cells bore clearly different sub-membrane mechanical structures. (
  • Cancer and normal cells exhibit different mechanical features because of the difference of their optical-microscopy defined actin cytoskeleton structures [4,19]. (
  • Our previous study showed that the regulatory mechanisms for actin cytoskeleton structures are different in normal stromal and cancer cells [20]. (
  • Filamentous actin or F-actin consists of long filamentous polymers of G-actin subunits. (
  • We show that the MAL RPEL domain binds actin more avidly than that of MC and that the RPEL motif itself is an actin-binding element. (
  • AFAP-110 binds actin filaments directly and multimerizes through a leucine zipper motif. (
  • Transmission electron microscopy of endocytic sites in F-actin binding mutants of S. cerevisiae suggest an absolute requirement for Vps1p to bind F-actin in order to generate directional propagation of an invaginations against the internal osmotic pressure of the cell. (
  • Each single ABD, comprising two CH domains, is able to bind one actin monomer in the filament. (
  • The N-terminal CH domain has the intrinsic ability to bind actin, albeit with lower affinity than the complete ABD, whereas the C-terminal CH bind actin extremely weakly or not at all. (
  • Expression of a deletion mutant of AFAP-110 that is unable to bind PKC blocked the effect of PMA on actin filaments. (
  • She and her team have been growing a mutant variety so they can better understand the cell's actin. (
  • A primary means by which F-actin transduces these signals is through its connections to focal adhesions and adherens junctions, which coordinate contact between the cell's actin cytoskeleton and either the extracellular matrix or another cell, respectively(Fig. 1). (
  • Induction of spine growth and synapse formation by regulation of the spine actin cytoskeleton. (
  • Actin binding by all three motifs is required for MAL regulation. (
  • Specifically, c-src-/- cells are deficient in several processes that require dynamic regulation of the actin cytoskeleton. (
  • Hyperglycemia causes neutrophil dysfunction by increasing intracellular calcium levels and interfering with actin and, thus, diapedesis and phagocytosis.Associated vaginal candidiasis and vascular disease also play a role in recurrent infections.SGLT2 inhibitors markedly increase glucose excretion by the kidney which may lead to a UTI. (
  • In light of novel discoveries related to the role and organization of neuronal F-actin, in this review we will focus on the mechanisms and molecular players that fine-tune the actin cytoskeleton, thereby controlling dendrite morphology and function. (
  • The cortical rigidity of mitotic round cells is less than that of trypsinized round cells despite of similar cell morphology and optical-microscopy visible actin networks [18]. (
  • For a long time, the most prominent roles that were attributed to actin in neurons were the movement of growth cones, polarized cargo sorting at the axon initial segment, and the dynamic plasticity of dendritic spines, since those compartments contain large accumulations of actin filaments (F-actin) that can be readily visualized using electron- and fluorescence microscopy. (
  • So far, research has been focused on the specific roles of actin in the axon, while it is becoming more and more apparent that in the dendrite, actin is not only confined to dendritic spines, but serves many additional and important functions. (
  • That once-elusive part, called actin, has long been known to play important roles in the cell. (
  • We found that the distribution of Myo2 in the AMR anticorrelates with the location of peeling events, suggesting that peeling is caused by a nonuniform tension distribution around the AMR, and that one of the roles of actin turnover is to maintain a uniform tension distribution around the AMR. (
  • In order to learn the relationship between characteristics and functional roles, actin genes from full-length cDNA library in Senecio scandens Buch. (
  • They are also known to cause changes in the organization of the actin cytoskeleton. (
  • Actin-accumulation myopathy is caused by a mutation in the ACTA1 gene. (
  • In some people with actin-accumulation myopathy, no ACTA1 gene mutations have been identified. (
  • Actin-accumulation myopathy is an autosomal dominant condition, which means one copy of the altered gene in each cell is sufficient to cause the disorder. (
  • Mutations and polymorphisms of the skeletal muscle alpha-actin gene (ACTA1). (
  • The β-actin gene is actively transcribed in all cell types and its promoter is highly enriched for histone modifications associated with active transcription, such as histone H3 Lys4 tri-methylation and general histone acetylation. (
  • This time he went looking for a gene that matures actin - and as a result, the skeleton of the cell. (
  • Functional Analysis of Actin Gene from Senecio scandens Buch. (
  • We propose that differential actin occupancy of multiple RPEL motifs regulates nucleocytoplasmic transport and activity of MAL. (
  • It does not react with actin from fibroblasts (beta- and gamma-cytoplasmic), striated muscle (alpha-sarcomeric) and myocardium (alpha-myocardial). (
  • ATP is a molecule that supplies energy for cells' activities, and is important in the formation of thin filaments from individual actin molecules . (
  • Microscopy image of actin. (
  • Therefore, the structural and regulatory differences of the apical actin filaments could be demonstrated by atomic force microscopy elasticity mapping analysis. (
  • Here, we use spectroscopic and structural techniques to determine how TRiC promotes the conformational progression of actin to the native state . (
  • In S. pombe , actin turnover is primarily regulated by the cofilin Adf1. (
  • In conjunction with MYOSINS , actin is responsible for the contraction and relaxation of muscle. (
  • So when Prachee Avasthi, Ph.D., and her team of researchers at the University of Kansas Medical Center shared information on one previously difficult-to-see part of an algal cell called actin, it flung open doors for scientific discovery. (
  • In fact, a major part of the work in Avasthi's lab reflects one amazing point: cilia, the antenna-like projections that grow on the outside of cell, need actin to form. (
  • Actin Filaments Arise from Nucleation Sites Usually in the Cell Cortex. (
  • Actin filaments are particularly abundant beneath the plasma membrane, where they form a network that provides mechanical support, determines cell shape, and allows movement of the cell surface, thereby enabling cells to migrate, engulf particles, and divide. (
  • Are actin filaments involved in cell division? (
  • Owing to its fundamental role in the cell, actin is a prominent regulator of cell division, a process, whose success directly depends on morphological changes of actin cytoskeleton and correct segregation of duplicated chromosomes. (
  • How is actin involved in cell division? (
  • Where are actin filaments located in the cell? (
  • Actin filaments are highly concentrated at the periphery of the cell, where they form a three-dimensional network beneath the plasma membrane(see Figure 11.6). (
  • Signaling pathways involving the Rho family of small GTPases mediate distinct actin cytoskeleton reorganization events in different cell types and have been proposed to be key mediators of dendritic development. (
  • Actin cytoskeleton remodeling and focal adhesion formation are associated with increased cell movement during epithelial to mesenchymal transition (EMT). (
  • Actin is yellow, cell core is blue). (
  • Actin cytoskeleton is indispensable for plant cell integrity. (
  • The cell mechanical features are largely regulated by actin cytokeleton. (
  • By analyzing the mechanical features, it is possible to evaluate the characteristics of the complicated actin cytoskeleton in diverse cell types. (
  • Dominant actin substructures differ by cell type as well as their subcellular localization. (
  • To give users a good overview which cell types have been already successfully stained with SiR-Actin and SiR-Tubulin, we are building up a data base in cooperation with Spirochrome. (
  • Cells were then analyzed by detecting the expression of epithelial cadherin (E-cadherin), collagen I, alpha smooth muscle cell actin (α-SMA), and activated Smads using Western blot. (
  • In order to examine the structure in cells, we have developed a computational technique that is able to probe the self-assembly of actin filaments through a lattice based Monte Carlo method. (
  • Recently, we have demonstrated that pre-treatment with actin disrupting drugs latrunculin B (latB) and cytochalasin E can enhance plant resistance against bacterial and fungal pathogens via activation of salicylic acid (SA) pathway. (
  • Pathway of Actin Folding Directed by the Eukaryotic Chaperonin TRiC. (
  • Both labs stained Human umbilical vein endothelial cells (HUVECs) either with SiR-Actin or with SiR-Tubulin. (
  • We can thus conclude that actin disruption itself triggers immune-like responses: there is an induction of SA via PAD4 coupled to ICS1;it leads to the induction of PR1 and WRKY38, and this requires a functional PI4K beta 1 beta 2 to be properly regulated. (