Actins: 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.Actin Cytoskeleton: Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.Actin Depolymerizing Factors: 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: Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Phalloidine: 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.Thiazolidines: Reduced (protonated) form of THIAZOLES. They can be oxidized to THIAZOLIDINEDIONES.Gelsolin: 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.Profilins: A family of low molecular weight proteins that bind ACTIN and control actin polymerization. They are found in eukaryotes and are ubiquitously expressed.Cytochalasin D: 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.Myosins: 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.Bicyclo Compounds, Heterocyclic: 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)Actin-Related Protein 2-3 Complex: 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.Contractile Proteins: 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.Pseudopodia: A dynamic actin-rich extension of the surface of an animal cell used for locomotion or prehension of food.Tropomyosin: A protein found in the thin filaments of muscle fibers. It inhibits contraction of the muscle unless its position is modified by TROPONIN.Cytoskeletal Proteins: 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.Actin-Related Protein 2: 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.Actin-Related Protein 3: 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.Rabbits: 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.Protein Binding: 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.Polymerization: Chemical reaction in which monomeric components are combined to form POLYMERS (e.g., POLYMETHYLMETHACRYLATE).Actomyosin: A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.Microscopy, Fluorescence: 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.Actinin: A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.Polymers: Compounds formed by the joining of smaller, usually repeating, units linked by covalent bonds. These compounds often form large macromolecules (e.g., BIOPOLYMERS; PLASTICS).Depsipeptides: Compounds consisting of chains of AMINO ACIDS alternating with CARBOXYLIC ACIDS via ester and amide linkages. They are commonly cyclized.Wiskott-Aldrich Syndrome Protein, Neuronal: 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.Biopolymers: 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.Wiskott-Aldrich Syndrome Protein: 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.rho GTP-Binding Proteins: 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 3.6.1.47.Cytochalasins: 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.Cell Movement: The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.Microscopy, Electron: 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.cdc42 GTP-Binding Protein: 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 3.6.1.47.Myosin Type II: 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.Muscles: Contractile tissue that produces movement in animals.Cells, Cultured: 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.Amino Acid Sequence: 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.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Filamins: 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.Vinculin: 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.Wiskott-Aldrich Syndrome Protein Family: 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.Viscosity: 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)Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Models, Biological: 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.Chickens: 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.Kinetics: The rate dynamics in chemical or physical systems.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Dictyostelium: 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.Cell Surface Extensions: Specialized structures of the cell that extend the cell membrane and project out from the cell surface.Microtubules: 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.rhoA GTP-Binding Protein: 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 3.6.1.47.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Signal Transduction: 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.Calmodulin-Binding Proteins: 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.rac1 GTP-Binding Protein: 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 3.6.1.47.rac GTP-Binding Proteins: 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 3.6.1.47.Green Fluorescent Proteins: 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.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Fibroblasts: Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.Cytochalasin B: A cytotoxic member of the CYTOCHALASINS.Recombinant Fusion Proteins: 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.Myosin Type I: 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.Protein Transport: 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.Mutation: 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.Microscopy, Confocal: 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.Myosin Type V: 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.Adenosine Triphosphate: 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.Fluorescent Antibody Technique: 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.Nucleic Acid Synthesis Inhibitors: Compounds that inhibit cell production of DNA or RNA.Tropomodulin: An actin capping protein that binds to the pointed-end of ACTIN. It functions in the presence of TROPOMYOSIN to inhibit microfilament elongation.Focal Adhesions: 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.Macromolecular Substances: 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.Calcium: 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.Cell Shape: The quality of surface form or outline of CELLS.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Muscle Proteins: The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.Phosphatidylinositol 4,5-Diphosphate: 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)Cytoplasm: 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)Thiazolesrho-Associated Kinases: 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.Molecular Motor Proteins: 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).Muscle, Smooth: 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)Amoeba: 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.Ca(2+) Mg(2+)-ATPaseModels, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Microscopy, Video: 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.Membrane Proteins: 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.Saccharomyces cerevisiae: 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.Cell Size: The quantity of volume or surface area of CELLS.Cross-Linking Reagents: 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.Calcium-Binding Proteins: Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.Protein Conformation: 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).PhosphoproteinsElectrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.GizzardRhodamines: 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 Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Myosin Heavy Chains: 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.Myofibrils: 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 .Zyxin: 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.Cytoplasmic Streaming: 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.Muscle, Skeletal: 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.Adenosine Triphosphatases: 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.Botulinum Toxins: 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.Saccharomyces cerevisiae Proteins: 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.Myosin Light Chains: The smaller subunits of MYOSINS that bind near the head groups of MYOSIN HEAVY CHAINS. The myosin light chains have a molecular weight of about 20 KDa and there are usually one essential and one regulatory pair of light chains associated with each heavy chain. Many myosin light chains that bind calcium are considered "calmodulin-like" proteins.Luminescent 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.Spectrin: 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.Time Factors: Elements of limited time intervals, contributing to particular results or situations.Paxillin: 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.HeLa Cells: 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.Cytokinesis: The process by which the CYTOPLASM of a cell is divided.Tubulin: 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.Deoxyribonuclease I: 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.Protein Multimerization: The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.Intercellular Junctions: 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)Transfection: 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.Epithelial Cells: 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.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Adaptor Proteins, Signal Transducing: 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 enzymesFluorescence Recovery After Photobleaching: 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).Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Fluorescent Dyes: 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.Troponin: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Time-Lapse Imaging: 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.Desmin: 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.Cattle: 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.Spectrometry, Fluorescence: Measurement of the intensity and quality of fluorescence.Cadherins: 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.Acanthamoeba: 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.Nerve Tissue ProteinsADP Ribose Transferases: 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.Enzyme Activation: 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.Molecular Weight: The sum of the weight of all the atoms in a molecule.Fungal Proteins: Proteins found in any species of fungus.Proteins: 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.Immunohistochemistry: Histochemical localization of immunoreactive substances using labeled antibodies as reagents.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Blotting, Western: 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.NIH 3T3 Cells: 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 http://www.atcc.org/)Adherens Junctions: 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.Marine Toxins: 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.Sarcomeres: The repeating contractile units of the MYOFIBRIL, delimited by Z bands along its length.Heterocyclic Compounds with 4 or More Rings: 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.3T3 Cells: 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.Wiskott-Aldrich Syndrome: 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.Vimentin: 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.Gels: 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.Cell Adhesion Molecules: 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.Pyrenes: A group of condensed ring hydrocarbons.Growth Cones: 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.COS Cells: 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).)Nonmuscle Myosin Type IIA: A nonmuscle isoform of myosin type II found predominantly in platelets, lymphocytes, neutrophils and brush border enterocytes.Intracellular Signaling Peptides and Proteins: 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.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Cell Membrane Structures: Structures which are part of the CELL MEMBRANE or have cell membrane as a major part of their structure.Stress, Mechanical: 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, Messenger: 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.Muscle, Striated: 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.Drosophila Proteins: 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.GTP Phosphohydrolases: Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.Fetal Proteins: Proteins that are preferentially expressed or upregulated during FETAL DEVELOPMENT.Cell Nucleus: 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)rhoB GTP-Binding Protein: 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 3.6.1.47.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.Muscle Contraction: 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.Cloning, Molecular: 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.Phosphatidylinositol Phosphates: Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.Microscopy, Electron, Scanning: 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.Cell Differentiation: Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.Two-Hybrid System Techniques: 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.Ethyldimethylaminopropyl Carbodiimide: Carbodiimide cross-linking reagent.Magnesium: 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.alpha Catenin: A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.Biophysical Phenomena: The physical characteristics and processes of biological systems.Potassium Chloride: 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.Gene Expression Regulation: 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.GTP-Binding Proteins: 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.-.Exocytosis: Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.Morphogenesis: 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.Protozoan Proteins: Proteins found in any species of protozoan.Biophysics: The study of PHYSICAL PHENOMENA and PHYSICAL PROCESSES as applied to living things.Myofibroblasts: 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.Immunoblotting: 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.Microinjections: The injection of very small amounts of fluid, often with the aid of a microscope and microsyringes.p21-Activated Kinases: 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.Chick Embryo: 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.RNA, Small Interfering: 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.Elasticity: Resistance and recovery from distortion of shape.Naphthalenesulfonates: A class of organic compounds that contains a naphthalene moiety linked to a sulfonic acid salt or ester.RNA Interference: 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.Lilium: 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.

Structural features of LIM kinase that control effects on the actin cytoskeleton. (1/626)

LIM kinase phosphorylates and inactivates the actin binding/depolymerizing factor cofilin and induces actin cytoskeletal changes. Several unique structural features within LIM kinase were investigated for their roles in regulation of LIM kinase activity. Disruption of the second LIM domain or the PDZ domain or deletion of the entire amino terminus increased activity in vivo measured as increasing aggregation of the actin cytoskeleton. A kinase-deleted alternate splice product was identified and characterized. This alternate splice product and a kinase inactive mutant inhibited LIM kinase in vivo, indicating that the amino terminus suppresses activity of the kinase domain. Mutation of threonine 508 in the activation loop to valine abolished activity whereas replacement with 2 glutamic acid residues resulted in a fully active enzyme. Dephosphorylation of LIM kinase inhibited cofilin phosphorylation. Mutation of the basic insert in the activation loop inhibited activity in vivo, but not in vitro. These results indicate phosphorylation is an essential regulatory feature of LIM kinase and indicate that threonine 508 and the adjacent basic insert sequences of the activation loop are required for this process. A combination of structural features are thus involved in receiving upstream signals that regulate LIM kinase-induced actin cytoskeletal reorganization.  (+info)

Ischemia activates actin depolymerizing factor: role in proximal tubule microvillar actin alterations. (2/626)

Apical membrane of renal proximal tubule cells is extremely sensitive to ischemia, with structural alterations occurring within 5 min. These changes are felt secondary to actin cytoskeletal disruption, yet the mechanism responsible is unknown. Actin depolymerizing factor (ADF), a 19-kDa actin-binding protein, has recently been shown to play an important role in regulation of actin filament dynamics. Because ADF is known to mediate pH-dependent F-actin binding, depolymerization, and severing, and because ADF activation occurs by dephosphorylation, we questioned whether ADF played a role in microvilli microfilament disruption during ischemia. To test our hypothesis, we induced renal ischemia in the rat with the clamp model. Initial immunofluorescence and Western blot studies on cortical tissue documented the presence of ADF in proximal tubule cells. Under physiological conditions, ADF was distributed homogeneously throughout the cytoplasm, primarily in the Triton X-100-soluble fraction, and both phosphorylated (pADF) and nonphosphorylated forms were identified. During ischemia, marked alterations occurred. Intraluminal vesicle/bleb structures contained extremely high concentrations of ADF along with G-actin, but not F-actin. Western blot showed a rapidly occurring duration-dependent dephosphorylation of ADF. At 0-30 min of ischemia, total ADF levels were unchanged, whereas pADF decreased significantly to 72% and 19% of control levels, at 5 and 15 min, respectively. Urine collected under physiological conditions did not contain ADF or actin, whereas urine collected after 30 min of ischemia contained both ADF and actin. Reperfusion was associated with normalization of cellular pADF levels, pADF intracellular distribution, and repair of apical microvilli. These data suggest that activation of ADF during ischemia via dephosphorylation is, in part, responsible for apical actin disruption resulting in microvillar destruction and formation of intraluminal vesicles.  (+info)

XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins. (3/626)

We carried out affinity column chromatography using Xenopus ADF/cofilin (XAC), identified several polypeptides in oocytes specifically bound to this column with actin, and isolated a full-length cDNA clone for a 65 kDa protein in this fraction. The predicted amino acid sequence revealed that the 65 kDa protein has seven obvious WD repeats and exhibits striking homology with yeast actin interacting protein 1 (AIP1). Thus, we designated this protein Xenopus AIP1 (XAIP1). We purified XAIP1 from Xenopus oocytes, and its interaction with actin was characterized by a pelleting assay, photometrical analysis and electron microscopy. Although XAIP1 itself cosedimented with F-actin and increased unsedimented actin to some extent, it induced a rapid, drastic disassembly of actin filaments associated with XAC. Electron microscopic observation revealed that XAIP1 severs actin filaments in the presence of XAC. To elucidate the in vivo effects of XAIP1, the purified protein was injected into blastomeres at the two-cell stage. Although the localization of XAIP1 was similar to that of XAC, at the cortical cytoskeleton and diffusely in the cytoplasm, injection of a large amount of XAIP1 arrested development and abolished the strong cortical staining of both actin and XAC. From these results, we concluded that XAIP1 regulates the dynamics of the cortical actin cytoskeleton cooperatively with XAC in eggs.  (+info)

Participation of cofilin in opsonized zymosan-triggered activation of neutrophil-like HL-60 cells through rapid dephosphorylation and translocation to plasma membranes. (4/626)

We studied the roles of cofilin, an actin-binding phosphoprotein, in superoxide production of neutrophil-like HL-60 cells triggered by opsonized zymosan (OZ). OZ caused dephosphorylation of cofilin as well as a transient increase of F-actin. Both reactions were complete within 30 s. Okadaic acid (OA) magnified the OZ-triggered O2--production 3.3-fold at 1 microM, but inhibited it completely at 5 microM. We used these critical concentrations to study the effects of OA on changes in phosphorylation and intracellular localization of cofilin. The OZ-induced dephosphorylation of cofilin was inhibited by 5 microM OA but not by 1 microM OA. Subcellular fractionation and immunoblotting revealed that 1 microM OA increased cofilin on the phagosomal membranous fraction but 5 microM OA decreased it. At 1 microM, OA increased translocation of p47phox to membranes, which may explain in part the enhancing effect of 1 microM OA. Confocal laser scanning microscopy showed that: (i) Cofilin diffused throughout the cytosol of resting cells, but accumulated at the plasma membranes forming phagocytic vesicles in activated cells. (ii) At 1 microM, OA had little effect on the OZ-evoked translocation of cofilin, whereas 5 microM OA suppressed it completely. (iii) OA alone, which could not trigger the phagocytic respiratory burst, did not cause any change in the distribution of cofilin at such concentrations. Furthermore, in a superoxide-producing cell-free system employing membranous and cytosolic fractions, affinity-purified anti-cofilin antibody showed an enhancing effect. These results suggest that cofilin participates in the superoxide production of the OZ-activated phagocytes through dephosphorylation and translocation. The roles of cofilin in the activated leukocytes will be discussed.  (+info)

UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle. (5/626)

The Caenorhabditis elegans unc-60 gene encodes two functionally distinct isoforms of ADF/cofilin that are implicated in myofibril assembly. Here, we show that one of the gene products, UNC-60B, is specifically required for proper assembly of actin into myofibrils. We found that all homozygous viable unc-60 mutations resided in the unc-60B coding region, indicating that UNC-60B is responsible for the Unc-60 phenotype. Wild-type UNC-60B had F-actin binding, partial actin depolymerizing, and weak F-actin severing activities in vitro. However, mutations in UNC-60B caused various alterations in these activities. Three missense mutations resulted in weaker F-actin binding and actin depolymerizing activities and complete loss of severing activity. The r398 mutation truncated three residues from the COOH terminus and resulted in the loss of severing activity and greater actin depolymerizing activity. The s1307 mutation in a putative actin-binding helix caused greater activity in actin-depolymerizing and severing. Using a specific antibody for UNC-60B, we found varying protein levels of UNC-60B in mutant animals, and that UNC-60B was expressed in embryonic muscles. Regardless of these various molecular phenotypes, actin was not properly assembled into embryonic myofibrils in all unc-60 mutants to similar extents. We conclude that precise control of actin filament dynamics by UNC-60B is required for proper integration of actin into myofibrils.  (+info)

Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments. (6/626)

We characterized the interaction of Acanthamoeba actophorin, a member of ADF/cofilin family, with filaments of amoeba and rabbit skeletal muscle actin. The affinity is about 10 times higher for muscle actin filaments (Kd = 0.5 microM) than amoeba actin filaments (Kd = 5 microM) even though the affinity for muscle and amoeba Mg-ADP-actin monomers (Kd = 0.1 microM) is the same (Blanchoin, L., and Pollard, T. D. (1998) J. Biol. Chem. 273, 25106-25111). Actophorin binds slowly (k+ = 0.03 microM-1 s-1) to and dissociates from amoeba actin filaments in a simple bimolecular reaction, but binding to muscle actin filaments is cooperative. Actophorin severs filaments in a concentration-dependent fashion. Phosphate or BeF3 bound to ADP-actin filaments inhibit actophorin binding. Actophorin increases the rate of phosphate release from actin filaments more than 10-fold. The time course of the interaction of actophorin with filaments measured by quenching of the fluorescence of pyrenyl-actin or fluorescence anisotropy of rhodamine-actophorin is complicated, because severing, depolymerization, and repolymerization follows binding. The 50-fold higher affinity of actophorin for Mg-ADP-actin monomers (Kd = 0.1 microM) than ADP-actin filaments provides the thermodynamic basis for driving disassembly of filaments that have hydrolyzed ATP and dissociated gamma-phosphate.  (+info)

Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. (7/626)

The leading edge (approximately 1 microgram) of lamellipodia in Xenopus laevis keratocytes and fibroblasts was shown to have an extensively branched organization of actin filaments, which we term the dendritic brush. Pointed ends of individual filaments were located at Y-junctions, where the Arp2/3 complex was also localized, suggesting a role of the Arp2/3 complex in branch formation. Differential depolymerization experiments suggested that the Arp2/3 complex also provided protection of pointed ends from depolymerization. Actin depolymerizing factor (ADF)/cofilin was excluded from the distal 0.4 micrometer++ of the lamellipodial network of keratocytes and in fibroblasts it was located within the depolymerization-resistant zone. These results suggest that ADF/cofilin, per se, is not sufficient for actin brush depolymerization and a regulatory step is required. Our evidence supports a dendritic nucleation model (Mullins, R.D., J.A. Heuser, and T.D. Pollard. 1998. Proc. Natl. Acad. Sci. USA. 95:6181-6186) for lamellipodial protrusion, which involves treadmilling of a branched actin array instead of treadmilling of individual filaments. In this model, Arp2/3 complex and ADF/cofilin have antagonistic activities. Arp2/3 complex is responsible for integration of nascent actin filaments into the actin network at the cell front and stabilizing pointed ends from depolymerization, while ADF/cofilin promotes filament disassembly at the rear of the brush, presumably by pointed end depolymerization after dissociation of the Arp2/3 complex.  (+info)

Aip1p interacts with cofilin to disassemble actin filaments. (8/626)

Actin interacting protein 1 (Aip1) is a conserved component of the actin cytoskeleton first identified in a two-hybrid screen against yeast actin. Here, we report that Aip1p also interacts with the ubiquitous actin depolymerizing factor cofilin. A two-hybrid-based approach using cofilin and actin mutants identified residues necessary for the interaction of actin, cofilin, and Aip1p in an apparent ternary complex. Deletion of the AIP1 gene is lethal in combination with cofilin mutants or act1-159, an actin mutation that slows the rate of actin filament disassembly in vivo. Aip1p localizes to cortical actin patches in yeast cells, and this localization is disrupted by specific actin and cofilin mutations. Further, Aip1p is required to restrict cofilin localization to cortical patches. Finally, biochemical analyses show that Aip1p causes net depolymerization of actin filaments only in the presence of cofilin and that cofilin enhances binding of Aip1p to actin filaments. We conclude that Aip1p is a cofilin-associated protein that enhances the filament disassembly activity of cofilin and restricts cofilin localization to cortical actin patches.  (+info)

Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. In the classical view, ADF/cofilin sever filaments, and capping proteins block filament barbed ends whereas pointed ends depolymerize, at a rate that is still debated. Here, by monitoring the activity of the three mammalian ADF/cofilin isoforms on individual skeletal muscle and cytoplasmic actin filaments, we directly quantify the reactions underpinning filament severing and depolymerization from both ends. We find that, in the absence of monomeric actin, soluble ADF/cofilin can associate with bare filament barbed ends to accelerate their depolymerization. Compared to bare filaments, ADF/cofilin-saturated filaments depolymerize faster from their pointed ends and slower from their barbed ends, resulting in similar depolymerization rates at both ends. This effect is isoform specific because depolymerization is faster for ADF- than for cofilin-saturated filaments. We also ...
Beads, bacteria and actin. Cofilin promotes rapid actin filament turnover in vivo. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
Marian Blanca Ramírez from the CSIC in Spain has been studying the effects of LRRK2, a protein associated with Parkinsons disease, on cell motility. A Travelling Fellowship from Journal of Cell Science allowed her to spend time in Prof Maddy Parsons lab at Kings College London, learning new cell migration assays and analysing fibroblasts cultured from individuals with Parkinsons. Read more on her story here. Where could your research take you? The deadline to apply for the current round of Travelling Fellowships is 30 Nov 2017. Apply now!. ...
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One candidate early on was a protein called slingshot, which seemed to have the correct phosphatase activity. However, slingshot turned out not to be found in all organisms, nor ubiquitously distributed throughout the body, a requirement for the mystery phosphatase, as it would be needed wherever actin dynamics is taking place. Additionally, slingshot did not appear to be capable of regulating all cofilin-dependent cell processes, so clearly a third man still existed.. Now in an article recently published in Nature Cell Biology, Bokoch and his colleagues Antje Gohla and Jörg Birkenfeld argue that the third man phosphatase is actually chronophin. Taking the increasingly overlooked approach of function-based biochemical isolation, which required Gohla to spend significant time in the cold room, the scientists purified a phosphatase activity which dephosphorylated cofilin. This activity was then identified by mass spectrometry as chronophin, a member of a unique superfamily of proteins called ...
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Cofilin belongs to the actin-binding ADF protein family. It contains one ADF-H domain. Cofilin controls reversible actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin at a 1:1 ratio. It is the major component of both intranuclear and cytop...
PAK4_HUMAN] Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of ...
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Actin-severing proteins ADF/cofilin are required for the sorting of secretory cargo at the trans-Golgi network (TGN) in mammalian cells. How do these cytoplasmic proteins interact with the cargoes in the lumen of the TGN ...
Garcia B, Stollar EJ, Davidson AR. Genetics. 2012 Aug;191(4):1199-211. Saccharomyces cerevisiae Actin-Binding Protein 1 (Abp1p) is a member of the Abp1 family of proteins, which are in diverse organisms including fungi, nematodes, flies, and mammals. All proteins in this family possess an N-terminal Actin Depolymerizing Factor Homology (ADF-H) domain, a central Proline-Rich Region (PRR), and a C-terminal SH3 domain. In this study, we employed sequence analysis to identify additional conservedfeatures of the family, including sequences rich in proline, glutamic acid, serine, and threonine amino acids (PEST), which are found in all family members examined, and two motifs, Conserved Fungal Motifs 1 and 2 (CFM1 and CFM2), that are conserved in fungi. We also discovered that, similar to its mammalian homologs, Abp1p is phosphorylated in its PRR. This phosphorylation is mediated by the Cdc28p and Pho85p kinases, and it protects Abp1p from proteolysis mediated by the conserved PEST sequences. We ...
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SSH3BP1小鼠单克隆抗体[4E2](ab11222)可与小鼠, 大鼠, 人样本反应并经WB, IP, IHC, ICC/IF实验严格验证,被9篇文献引用。所有产品均提供质保服务,中国75%以上现货。
SSH2兔多克隆抗体(ab118079)可与重组片段样本反应并经WB, IP实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
2019- 2020學年(上學期)????? (2019.10.14-2019.10.18)課題組名稱(聯系人)時? 間地? 點主講人題?? 目理論物理研究所 (李世淵)星期三15:30知新樓C913??交叉科學研究所 (劉向東)星期二下午離子束報告廳????????原子分子物理 (許國富)星期三下午知新樓C1011??????????凝聚態理論研究室 (崔彬)星期四14:30知新樓C1113季藝聞基于SSH模型對A-D-A類分子建模????電介質物理研究室 (趙明磊)星期五14:30知新樓C1113??...
For the SSH-1 protocol, see Secure Shell#Version 1.x Protein phosphatase Slingshot homolog 1 is an enzyme that in humans is encoded by the SSH1 gene. The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin dynamics. ADF/cofilin proteins are inactivated by kinases such as LIM domain kinase-1 (LIMK1; MIM 601329). The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[supplied by OMIM] GRCh38: Ensembl release 89: ENSG00000084112 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000042121 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (Apr 2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65-73. doi:10.1093/dnares/7.1.65. PMID 10718198. Niwa ...
Having identified changes in the extent of cofilin phosphorylation in cells at steady state, we next examined the dynamics of cofilin phosphorylation in cells undergoing acute changes in actin cytoskeletal organisation. This required the identification of a stimulus able to induce dynamic actin remodelling. In testing a number of growth factors in S2R+ cells [10% foetal calf serum (FCS), 2-day-old conditioned medium, bovine insulin, human EGF, murine vascular endothelial growth factor (VEGF) and human platelet-derived growth factor (PDGF)], only insulin was found to activate signalling, as monitored by immunoblotting with specific antibodies against P-Akt, S6K phosphorylated at Thr398 (P-S6K) and ERK phosphorylated at Thr198 and Tyr200 (PP-ERK) (supplementary material Fig. S3A) and Lizcano et al. (Lizcano et al., 2003). Insulin also induced an increase in the level of lamellipodial F-actin in these cells within 5 minutes of treatment (Fig. 2A). Elevated levels of filamentous actin remained at ...
During early metastatic events in cancer, reorganization of the actin cytoskeleton must occur to allow for cell invasion and migration. A key enzyme initiating actin remodeling at the leading edge is Cofilin, a small actin binding protein of the ADF/cofilin family with actin severing activities. Cofilin activity is tightly regulated by phosphorylation and dephosphorylation events that are mediated by LIM Kinase (LIMK) and the phosphatase Slingshot (SSH), respectively. Protein kinase D (PKD) is a serine/threonine kinase that has previously been shown to regulate actin driven directed cell migration through phosphorylation and thus inactivation of Slingshot. Here we show that PKD can also regulate cofilin activity via activation of LIMK. We further show that PKD-induced regulation of LIMK and the resulting diminished cofilin activity translates to altered cell motility. Our data suggest that PKD inactivates Cofilin through modulation of both of its regulatory pathways. Further elucidation of the ...
Cofilin 1 (non-muscle; n-cofilin), also known as CFL1, is a human gene, part of the ADF/cofilin family. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus. One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration. Cofilin 1 has been shown to interact with HSPH1 and LIMK1. GRCh38: Ensembl release 89: ENSG00000172757 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000056201 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". "Entrez Gene: CFL1 cofilin 1 (non-muscle)". Chai X, Förster E, Zhao S, Bock HH, Frotscher M (January 2009). "Reelin stabilizes the actin cytoskeleton of neuronal processes by inducing n-cofilin ...
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
The actin depolymerizing factor (ADF)/cofilin protein family is essential for actin dynamics, cell division, chemotaxis and tumor metastasis. Cofilin-1 (CFL-1) is a primary non-muscle isoform of the ADF/cofilin protein family accelerating the actin filamental turnover in vitro and in vivo. In response to environmental stimulation, CFL-1 enters the nucleus to regulate the actin dynamics. Although the purpose of this cytoplasm-nucleus transition remains unclear, it is speculated that the interaction between CFL-1 and DNA may influence various biological responses, including DNA damage repair. In this review, we will discuss the possible involvement of CFL-1 in DNA damage responses (DDR) induced by ionizing radiation (IR), and the implications for cancer radiotherapy.
Cofilin phospho-regulation is important for actin filament turnover and is implicated in cancer. Phosphorylation of cofilin is mediated by LIM kinases (LIMKs) and dephosphorylation by Slingshot phosphatases (SSH). LIMKs and SSH promote cancer cell invasion and metastasis and represent novel anti-cancer targets. However, little is known regarding LIMK/cofilin and SSH in human colorectal cancer (CRC). In this study, we aimed to address their expression and significance in human CRC. We evaluated expression of non-phosphorylated (active) and phosphorylated cofilin, LIMK1, LIMK2, and SSH1 by immunohistochemistry in 143 human CRC samples in relation to clinicopathologic parameters, response of metastatic disease to chemotherapy, and epithelial-mesenchymal transition (EMT) markers β-catenin, E-cadherin, and ZEB ...
The severing of filaments by ADF/cofilins was originally proposed for the following reasons: It was first noticed that ADF accelerated actin polymerization and promoted a rapid drop in fluorescence of NBD- or pyrenyl-labeled F-actin (Cooper et al., 1986; Maciver et al., 1991; Moon et al., 1993; Quirk et al., 1993; Maciver and Weeds, 1994), but both properties were interpreted in terms of an increase in filament number due to fragmentation. The fragmentation hypothesis was enticing because it also provided a satisfactory explanation for the rapid drop in viscosity of F-actin solutions after addition of substoichiometric amounts of ADF, similar to the effect of the severing protein gelsolin. Further effort was made to visualize the fragmentation in electron or optical microscopy. In some instances, filaments were observed to be shorter, which was thought to be because of depolymerization (Abe and Obinata, 1989) or severing (Cooper et al., 1986). In other instances, filaments did not appear shorter ...
The presence of LIMK activity in retina was demonstrated with Western blot and immunocytochemistry. With confocal microscopy we observed the localization of p-LIMK in rod axon terminals, precisely the area that undergoes dramatic morphologic change after retinal dissociation. Measuring the reduction in axon length allowed us to demonstrate the prevention of axonal retraction by inhibiting LIMK. Furthermore, inhibiting LIMK upstream regulators, ROCK and Pak, increased inhibition of axonal retraction, and the two pathways demonstrated an additive effect. The involvement of ROCK is not surprising, as we have previously demonstrated that inhibiting the RhoA-ROCK pathway can block axonal retraction.15,16 ROCK has been reported to be responsible for actomyosin contractility as well as actin filament turnover (Fig. 1).19,20,35-37 Blocking its activity therefore presumably reduces both contraction and actin filament turnover. Pak has been reported to regulate formation of filopodia and lamellipodia via ...
Cell motility plays an important role in many basic biological processes, including embryogenesis, neurite growth, wound healing, inflammation, and cancer metastasis. Motility of crawling cells is dependent on the ability to extend F-actin-rich protrusions, usually in the form of lamellipods (Abercrombie et al. 1970; Chen et al. 1994; Verschueren et al. 1994; Xie et al. 1995). Protrusion of such actin-rich lamellipods in moving cells requires cycles of actin polymerization and depolymerization (actin polymerization transients) (Lauffenburger and Horwitz 1996; Mitchison and Cramer 1996; Bailly et al. 1998a; Condeelis 1998).. Previous studies have demonstrated the requirement for free barbed ends in the control of this cycle (Handel et al. 1990; Symons and Mitchison 1991; Chan et al. 1998). We have shown previously that stimulation of metastatic MTLn3 cells with EGF causes a transient increase in actin nucleation activity resulting from the appearance of free barbed ends at the extreme leading ...
A model from Chile, Maura Bellagamba, released a video on Instagram of herself being released in a giant slingshot, which she says caused her neck injuries while filming a Nissan car commercial.. Bellagamba wrote on Instagram that she was fired out of the slingshot without her permission, causing her whiplash ...
Serotonin (5-HT) is known to increase the rate of growth cone advance via cofilin-dependent increases in retrograde actin network flow and nonmuscle myosin II activity ...
FtsZ filament dynamics at steady state: subunit exchange with and without nucleotide hydrolysis.s profile, publications, research topics, and co-authors
To confirm the morphological effects of 5-HT6Rs transfected in neuronal cells, we finally examined whether the activation of neuronal 5-HT6Rs produces effects on RhoA activities. To perform RhoA activity assay as shown in Fig. 2, we carried immunoblot analysis using cultured cortical neurons for sufficient amount of sample proteins. Here, we showed that 5-HT6R activation by ST1936 significantly increased RhoA-GTP level, which was significantly blocked by the pretreatment with SB258585 in cultured neurons (Figs. 4A and 4B). As downstream targets of Rho proteins, RhoA proteins can also affect actin polymerization by regulating cofilin via Rho-ROCK-LIMK-cofilin pathway (Lin et al., 2003). Therefore, we further executed whether the activation of 5-HT6Rs modulates cofilin activities as a downstream target of RhoA. As shown in Figs. 4C and 4D, we observed that treatment with ST1936 significantly increased phosphorylation of cofilin, which was also significantly blocked by SB258585 in cultured neurons. ...
To confirm the morphological effects of 5-HT6Rs transfected in neuronal cells, we finally examined whether the activation of neuronal 5-HT6Rs produces effects on RhoA activities. To perform RhoA activity assay as shown in Fig. 2, we carried immunoblot analysis using cultured cortical neurons for sufficient amount of sample proteins. Here, we showed that 5-HT6R activation by ST1936 significantly increased RhoA-GTP level, which was significantly blocked by the pretreatment with SB258585 in cultured neurons (Figs. 4A and 4B). As downstream targets of Rho proteins, RhoA proteins can also affect actin polymerization by regulating cofilin via Rho-ROCK-LIMK-cofilin pathway (Lin et al., 2003). Therefore, we further executed whether the activation of 5-HT6Rs modulates cofilin activities as a downstream target of RhoA. As shown in Figs. 4C and 4D, we observed that treatment with ST1936 significantly increased phosphorylation of cofilin, which was also significantly blocked by SB258585 in cultured neurons. ...
Fads remind me of an iPad game called Slingshot Racing. What you do is, there are these tiny cars that run around a tiny oval racetrack, and you have to click on the screen (tech faux pas! tap on the screen) to tether the cars to tiny towers that slingshot them around the corners (ends? short sides?) of the oval. It sounds easy but in fact its devastatingly hard to tap and release at exactly the right times to start the tether and stop it without smashing your tiny car into a tiny wall. Thats kind of like catching and riding a fad. You have to discover that the potential for a fad exists, and not just any fad; one you can make money on, say by selling rocks or playing the saxophone in a particular way. You have to tether the fad to you at just the right moment, then hold onto it just up until the moment when its about to fade, at which point you release it before you start looking stupid. Few succeed at this game. Some tap too early and suffer ridicule, that is, until after theyre dead and ...
If you know of any papers that use this antibody, please contact us at antibodies [at] alzforum [dot] org for consideration in the References section.. ...
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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 ...
The characterization of novel therapeutic antibodies with multivalent or multispecific binding sites requires new measurement modalities for biosensors, to discriminate the engagement of antigens via one, two, or even more binding moieties. The presentation of antigens on a sensor surface in a well-controlled spatial arrangement is a prerequisite for the successful interpretation of binding kinetics measurements of multivalent analytes, but the adjustment of defined distances between immobilized ligands is difficult to achieve in state-of-the-art biosensor systems. Here, we introduce a simple DNA nanostructure resembling a slingshot, which can be configured with two identical or two different antigens (bivalent or bispecific), which are spaced at a defined distance. We characterize the slingshot structure with a chip-based biosensor using electrically switchable DNA nanolevers and demonstrate that bivalent and monovalent antibodies selectively interact with slingshots that have been ...
Drosophila S2 cells offer a powerful tool to study in vivo dynamics and organization of the actin cytoskeleton. When plated on the lectin, concanavalin A, S2 cells attach and spread on the substrate to form a circumferential actin-based lamellae. The susceptibility of these cells to gene inhibition using RNAi makes them a very tractable system to dissect the molecular machinery involved in lamellipod formation. The figure shows a control S2 (upper left) in comparison with cells depleted of capping protein beta (upper right), cofilin (lower left), and Rho1 (lower right). The hyper-ruffled morphology produced by capping protein RNAi is consistent with its role in terminating actin filament elongation - in the absence of the protein, actin filaments polymerization pushes on the membrane in an unregulated manner. Depletion of cofilin, a factor required for actin filament turnover, produces cells that are unable to spread due to abnormal accumulations of f-actin at their cortex. RNAi-inhibition of ...
1PEV: Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.
The coordination of cell polarity within the plane of the tissue layer (planar polarity) is crucial for the development of diverse multicellular organisms. Small Rac/Rho-family GTPases and the actin cytoskeleton contribute to planar polarity formation at sites of polarity establishment in animals and plants. Yet, upstream pathways coordinating planar polarity differ strikingly between kingdoms. In the root of Arabidopsis thaliana, a concentration gradient of the phytohormone auxin coordinates polar recruitment of Rho-of-plant (ROP) to sites of polar epidermal hair initiation. However, little is known about cytoskeletal components and interactions that contribute to this planar polarity or about their relation to the patterning machinery. Here, we show that ACTIN7 (ACT7) represents a main actin isoform required for planar polarity of root hair positioning, interacting with the negative modulator ACTIN-INTERACTING PROTEIN1-2 (AIP1-2). ACT7, AIP1-2 and their genetic interaction are required for ...
In the fall of 2017, NPR Music and VuHaus' public radio network kicked off Slingshot, a collaboration among taste-making music radio stations to
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The discussion focuses specifically on imaging cytoskeletal molecules- actin and microtubulues, filmanets that can polymerize on one end and depolymerize on the other. Spindles were imaged by first labeling them with a fluorescent dye that attached to the individual tubulin molecules and then imaging using spinning-disk confocal microscopy. Taking movies of the system reveals that the tubulin molecules are in constant movement. To perform data analysis one needs to carry out particle tracking. To do this, particles must first be identified in each time frame, and then must be linked from frame to frame in order to create a trajectory for each particle. ...
Genes encoding the various isoforms of actin. In Drosophila, for example, actin genes have been localized at six different chromosomal sites. Two genes encode cytoplasmic actins, while the other four encode muscle actins. The amino acid- encoding segments of the different actin genes have very similar compositions, but the segments specifying the trailers (q.v.) differ considerably in nucleotide sequences. ...
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Figure 1: Ultra-Pure Actin is ,90% polymerization-competent. Ultra-Pure Actin was polymerized in the absence (-PB) or presence (+PB) of Actin Polymer Buffer (10X, Cat. No. 000103; 50 mM KCl and 2 mM MgCl2) followed by centrifugation at 48k rpm for 1 hour. Pellet (P) and supernatant (S) fractions were collected and subjected to SDS-PAGE and Coomassie G250-staining. >90% of Ultra-Pure Actin was incorporated into filaments as determined by measuring the residual protein concentration in the supernatant fraction.. ...
Figure 1. Model for the regulation of actin cytoskeletal dynamics by mTORC2. Activation of PKC by mTORC2 results in a phosphorylation of GAP-43-like proteins,
The latter is the enzyme that uses ATP to phosphorylate and inactivate the actin-depolymerizing factor cofilin. When cofilin is ... LIMK1 also depolymerizes microtubules. In the presence of Pyr1, LIMK1 is inhibited, which means that the phosphorylation of ... Pyr1 may be used in cancer treatment, because its main target enzyme (LIM kinase) is a regulator of microtubule and actin ... In conclusion, Pyr1 inhibits cell motility and controls actin dynamics and stabilizes microtubules. These properties can be ...
The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin ... Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T (Feb 2002). "Control of actin reorganization by Slingshot, a family of ... 2006). "Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L". FEBS Lett. 580 (7): 1789-94. doi: ... The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[ ...
The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of ... This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin ... "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985-93. doi: ... Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene. ...
2003). "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/ ... Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to ... Palmgren S, Vartiainen M, Lappalainen P (2002). "Twinfilin, a molecular mailman for actin monomers". J. Cell Sci. 115 (Pt 5): ... 2003). "The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers". Mol. Biol. ...
"NMR assignments of actin depolymerizing factor (ADF) like UNC-60A and cofilin like UNC-60B proteins of Caenorhabditis elegans ...
The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin ... The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[ ... "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin". Cell. 108 (2): 233-46 ...
While the repulsive cue, Slit, is suggested to stimulate the translation of Cofilin (an actin depolymerizing factor) in growth ... 2006). "Asymmetrical β-actin mRNA translation in growth cones mediates attractive turning to netrin-1". Nature Neuroscience. 9 ... The attractive cue Netrin-1, stimulates mRNA transport and influence synthesis of β-Actin in filopodia of growth cones, to ... and L1 Growth factors like NGF Neurotransmitters and modulators like GABA Growing axons rely on a variety of guidance cues in ...
"The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics". ... Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and ... Bamburg JR, McGough A, Ono S (September 1999). "Putting a new twist on actin: ADF/cofilins modulate actin dynamics". Trends ... 2006). "Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface". J. Mol. Biol. ...
... also known as ADF or actin depolymerizing factor Actin-binding proteins regulate assembly and disassembly of actin filaments. ... March 1997). "Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based ... ATP-actin is then available for assembly. Cofilin binds monomeric (G-actin) and filamentous actin (F-actin). Its binding ... "Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in ...
... inhibiting its actin-depolymerizing activity. This depolymerization results in stabilization of actin filaments and decreased ... Gilkes DM, Xiang L, Lee SJ, Chaturvedi P, Hubbi ME, Wirtz D, Semenza GL (January 2014). "Hypoxia-inducible factors mediate ... It is a key regulator of actin-myosin contraction, stability, and cell polarity. These contribute to many progresses such as ... This is consistent with its function as a key modulator of cell motility, tumor cell invasion, and actin cytoskeleton ...
Actin depolymerizing factors MeSH D05.750.078.730.212.500 --- cofilin 1 MeSH D05.750.078.730.212.750 --- cofilin 2 MeSH D05.750 ... actin-related protein 2 MeSH D05.750.078.730.246.750 --- actin-related protein 3 MeSH D05.750.078.730.250 --- actins MeSH ... actin capping proteins MeSH D05.750.078.730.032.500 --- capz actin capping protein MeSH D05.750.078.730.032.750 --- ... 212.875 --- destrin MeSH D05.750.078.730.246 --- actin-related protein 2-3 complex MeSH D05.750.078.730.246.500 --- ...
"Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin". J ... ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin ... In molecular biology, ADF-H domain (actin-depolymerising factor homology domain) is an approximately 150 amino acid motif that ... They bind both actin-monomers and filaments and promote rapid filament turnover in cells by depolymerising/fragmenting actin ...
Actin depolymerizing factors are a family of microfilament proteins. They are used to regulate actin assembly. Actin ... "Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover". J. Biol. Chem. 273 (40 ... Depolymerizing Factors at the US National Library of Medicine Medical Subject Headings (MeSH) Didry D, Carlier MF, Pantaloni D ... "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009-19. doi: ...
Actin Depolymerizing Factor, or ADF, normally disassembles actin and does not allow for the induction of LTP. However, synaptic ... Actin treadmilling is the process of turnover of actin filaments where F-actin is rapidly assembled and disassembled. G-actin ... This protein caps the barbed end of F-actin, thus blocking G-actin subunits to bind to the F-actin and allow for actin ... Actin is only able to cause changes that promote LTP through its formation into F-actin. When F-actin is unable to form, LTD is ...
actin cytoskeleton. • extracellular exosome. • stress fiber. • plasma membrane. • Z disc. • cytoplasm. • cell cortex. • focal ... actin binding. • RNA binding. • cadherin binding. Cellular component. • integral component of membrane. • cytoskeleton. • brush ... actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... Filamin B, beta (FLNB), also known as Filamin B, beta (actin binding protein 278), is a cytoplasmic protein which in humans is ...
actin cytoskeleton. • extracellular exosome. • cytoskeleton. • cytosol. • actin filament. • phagocytic vesicle. Biological ... MBInfo - WASP and other Nucleation Promotion Factors. *GeneReviews/NIH/NCBI/UW entry on WAS-Related Disorders including Wiskott ... actin filament-based movement. • endosomal transport. • actin filament polymerization. • regulation of T cell antigen ... actin binding. • protein kinase binding. • small GTPase binding. • Rac GTPase binding. Cellular component. • cytoplasm. • cell- ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... Ras guanyl-nucleotide exchange factor activity. • protein domain specific binding. • phospholipase binding. • structural ... Pospelov VA, Pospelova TV, Julien JP (February 1994). "AP-1 and Krox-24 transcription factors activate the neurofilament light ...
... actin. Each F actin strand is composed of a string of subunits called globular (G) actin. Each G actin has an active site that ... The filaments of actin and myosin then form linkages. After binding, myosin pulls actin filaments toward each other, or inward ... actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... Myofilaments are the filaments of myofibrils, constructed from proteins,[1] principally myosin or actin. Types of muscle are ...
actin binding. • motor activity. • ATP binding. • RNA binding. • cadherin binding. • actin filament binding. • microtubule ... Li ZH, Bresnick AR (May 2006). "The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin- ... actin cytoskeleton reorganization. • regulation of cell shape. • actin filament-based movement. • platelet aggregation. • ... Other proteins that are known to interact with NM IIA include the actin binding protein tropomyosin 4.2 [26] and a novel actin ...
... that links the actin cytoskeleton to adhesion proteins.[8][9] In addition to F-actin,[10] the N-terminal region of talin-1 ... actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... actin filament binding. • LIM domain binding. • integrin binding. • protein binding. • vinculin binding. • protein complex ... actin binding. • cadherin binding. • phosphatidylserine binding. • phosphatidylinositol binding. Cellular component. • ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... It also functions as a recruiting factor that localizes dynein to where it should be.[14][15] There is also some evidence ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... which is clinically important because elevated expression of the sodium calcium exchanger is a factor related to arrhythmia and ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... Association with actin and desmin filaments". Circulation Research. 71 (2): 288-94. doi:10.1161/01.res.71.2.288. PMID 1628387. ...
actin depolymerizing factors *Cofilin *1. *2. *Destrin. *Gelsolin. *Profilin *1. *2. *Titin ... actin binding. • tropomyosin binding. • troponin I binding. • calcium-dependent protein binding. • troponin C binding. • ...
actin filament bundle assembly. • positive regulation of neuron apoptotic process. • vascular endothelial growth factor ... Miki H, Sasaki T, Takai Y, Takenawa T (January 1998). "Induction of filopodium formation by a WASP-related actin-depolymerizing ... "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin- ... actin cytoskeleton organization. • regulation of filopodium assembly. • endocytosis. • ephrin receptor signaling pathway. • ...
Actin depolymerizing factors are a family of microfilament proteins. They are used to regulate actin assembly. Actin ... "Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover". J. Biol. Chem. 273 (40 ... Depolymerizing Factors at the US National Library of Medicine Medical Subject Headings (MeSH) Didry D, Carlier MF, Pantaloni D ... "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009-19. doi: ...
Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, ... Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, ... Structure of the actin-depolymerizing factor homology domain in complex with actin. Paavilainen, V.O., Oksanen, E., Goldman, A. ... Structure of the actin-depolymerizing factor homology domain in complex with actin. *DOI: 10.2210/pdb3DAW/pdb ...
... an important regulator of actin cytoskeleton, in the oxidized low-density lipoprotein (ox-LDL)-induced... ... The aim of present work was to elucidate the role of actin-depolymerizing factor (ADF), ... Actin-depolymerizing factor Endothelial Blood-brain barrier Reactive oxygen species Actin cytoskeleton ... The aim of present work was to elucidate the role of actin-depolymerizing factor (ADF), an important regulator of actin ...
Competes with unc-87 for actin binding and inhibits the actin-bundling activity of unc-87 (PubMed:17684058). ... required for the assembly of actin filaments into the functional contractile myofilament lattice of muscle (PubMed:8107682). ... sp,Q07750,ADF1_CAEEL Actin-depolymerizing factor 1, isoforms a/b OS=Caenorhabditis elegans OX=6239 GN=unc-60 PE=1 SV=2 ... Depolymerizes growing actin filaments in muscle cells; required for the assembly of actin filaments into the functional ...
Cofilin-1 (CFL-1) is a primary non-muscle isoform of the ADF/cofilin protein family accelerating the actin filamental turnover ... In response to environmental stimulation, CFL-1 enters the nucleus to regulate the actin dynamics. Although the purpose of this ... cofilin protein family is essential for actin dynamics, cell division, chemotaxis and tumor metastasis. ... The actin depolymerizing factor (ADF)/cofilin protein family is essential for actin dynamics, cell division, chemotaxis and ...
The main function of ADF is the severing and depolymerizing filamentous actin (F-actin), thus regulating F-actin... ... ACTIN DEPOLYMERIZING FACTOR (ADF) is a conserved protein among eukaryotes. ... Actin interacting protein1 and actin depolymerizing factor drive rapid actin dynamics in Physcomitrella patens. Plant Cell 23: ... Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin ...
"Actin Depolymerizing Factors" by people in this website by year, and whether "Actin Depolymerizing Factors" was a major or ... "Actin Depolymerizing Factors" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH ( ... Below are the most recent publications written about "Actin Depolymerizing Factors" by people in Profiles. ... Below are MeSH descriptors whose meaning is more general than "Actin Depolymerizing Factors". ...
Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol ... Hawkins M, Pope B, Maciver SK, Weeds AG (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin ... Mehta S, Sibley LD (2010) Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J Biol Chem 285(9 ... Funk JD, Bamburg JR (2007) Proteins of the actin depolymerizing factor/Cofilin family. In: Actin-monomer-binding proteins. ...
2002 The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics ... Actin Depolymerizing Factors Cofilin1 and Destrin Are Required for Ureteric Bud Branching Morphogenesis Download PDF České info ... proLékaře.cz / Odborné časopisy / PLOS Genetics / 2010 - 10 / Actin Depolymerizing Factors Cofilin1 and Destrin Are Required ... 2005 The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev ...
Recombinant Protein and Actin-depolymerizing factor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody ... Actin-depolymerizing factor 1. Actin-depolymerizing factor 1 ELISA Kit. Actin-depolymerizing factor 1 Recombinant. Actin- ... Actin-depolymerizing factor 10. Actin-depolymerizing factor 10 ELISA Kit. Actin-depolymerizing factor 10 Recombinant. Actin- ... Actin-depolymerizing factor 11. Actin-depolymerizing factor 11 ELISA Kit. Actin-depolymerizing factor 11 Recombinant. Actin- ...
They remodel the actin CYTOSKELETON by severing ACTIN FILAMENTS and increasing the rate of monomer dissociation. ... A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. ... Actin Depolymerizing Factors. Known as: ADF Proteins (Actin Depolymerizing Factors), Actin Depolymerizing Proteins, Cofilins ... The ADF (actin-depolymerizing factor)/cofilin family is a stimulus-responsive mediator of actin dynamics. In contrast to the… ...
Actin-depolymerizing factor 5 - Also known as ADF5_ORYSJ, ADF5. Actin-depolymerizing protein. Severs actin filaments (F-actin) ... Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (By similarity). ... Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (By similarity). ... and binds to actin monomers (By similarity). ... Actin-depolymerizing factor 5. MOLECULAR SYNOPSIS. STRUCTURAL ...
Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte architecture. Journal of Biological Chemistry ... Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte architecture. / Garg, Puneet; Verma, Rakesh; ... Fingerprint Dive into the research topics of Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte ... title = "Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte architecture", ...
actin-depolymerizing factor. *ADF. *AGEL. *brevin. *DKFZp313L0718. *GELS_HUMAN. *gelsolin isoform a precursor ... Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, ... to another protein called actin. Actin proteins are organized into filaments, which form a network (the cytoskeleton) that ... Gelsolin helps assemble or disassemble actin filaments. It is thought that, through this function, the gelsolin protein ...
Actin depolymerizing factor (ADF), a 19-kDa actin- binding protein, has recently been shown to play an important role in ... Actin depolymerizing factor (ADF), a 19-kDa actin- binding protein, has recently been shown to play an important role in ... Actin depolymerizing factor (ADF), a 19-kDa actin- binding protein, has recently been shown to play an important role in ... Actin depolymerizing factor (ADF), a 19-kDa actin- binding protein, has recently been shown to play an important role in ...
1993) Isolation and characterization of a regulated form of actin depolymerizing factor. J Cell Biol 122:623-633, doi:10.1083/ ... Cofilin, the major actin depolymerizing factor, is required for Shank3 regulation of NMDAR currents.. Next, we examined the ... 1995) Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270: ... Inhibiting cofilin, the primary downstream target of PAK and a major actin depolymerizing factor, prevented Shank3 siRNA from ...
... aspb.org The interior of a plant cell is supported by the actin cytoskeleton, a complex network of yarn-like fibers… ... such as actin depolymerizing factors (ADFs). ADFs can bind to both monomeric and filamentous actin (F-actin). Across the plant ... Loose-Knit Family: Tracing the Evolution of Actin Depolymerizing Factors that Sever or Join the Actin Cytoskeleton January 31, ... depolymerizing F-actin) ADFs, which sever or depolymerize F-actin and 2) B-type (bundling F-actin) ADFs, which bind to and ...
... are small actin-binding proteins. Many higher-plant ADFs has been known to involve in plant growth, development and pathogen ... Actin depolymerizing factors (ADFs) are small actin-binding proteins. Many higher-plant ADFs has been known to involve in plant ... Staiger CJ, Gibbon BC, Kovar DR, Zonia LE: Profilin and actin-depolymerizing factor: modulators of actin organization in plants ... Actin-depolymerizing factor 2-mediated actin dynamics are essential for root-knot nematode infection of Arabidopsis. Plant Cell ...
T. gondii actin depolymerizing factor (TgADF) plays an important role in actin cytoskeleton remodeling, and it is required to ... T. gondii actin depolymerizing factor (TgADF) plays an important role in actin cytoskeleton remodeling, and it is required to ... Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii. Mol Biol Cell. 2011;22:1290-9. ... Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J Biol Chem. 2010;285:6835-47. ...
A Mechanism for Actin Filament Severing by Malaria Parasite Actin Depolymerizing Factor 1 via a Low Affinity Binding Interface ...
Cofilin/actin-depolymerizing factor homolog 1. Plasmodium falciparum (isolate HB3) ... Cofilin/actin-depolymerizing factor homolog 1 UniProtKBInterProInteractive Modelling. 122 aa; Sequence (Fasta) 14 identical ... Crystal Structure of an Actin Depolymerizing Factor. monomer 2×TAR; 2×BME;. 3q2b. 2-121. ... Crystal structure of Plasmodium falciparum actin depolymerization factor 1. homo-2-mer 8×SO4;. 2xf1. 1-120. ...
Actin Depolymerizing Factors * Epidermal Growth Factor Grant support * P01 CA100324/CA/NCI NIH HHS/United States ...
Overexpression of actin-depolymerizing factor blocks oxidized low-density lipoprotein-induced mouse brain microvascular ... to cause barrier disruption in mice which has been attributed to a decrease in the expression of actin-depolymerizing factor ( ... To determine whether the increase in cytokine secretion was due to activation of NF-KB (nuclear factor kappa-light-chain- ... cardiovascular comorbidities and risk factors [19]. Three patients in the AD group were diagnosed with hypertension alone. ...
Actin depolymerizing factor. *ADF. *AGEL. *Brevin. *Gelsolin. see all. * Relevance. Gelsolin is a calcium regulated, actin ... and severs actin filaments in the presence of submicromolar calcium, thereby solating cytoplasmic actin gels. A calcium ... It plays a role in phosphoinositide mediated disassembly of actin filaments in Sertoli cell adhesion complexes; it may regulate ... modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end ...
0 (Actin Depolymerizing Factors); 0 (Microfilament Proteins); 0 (Wdr1 protein, mouse); EC 2.7.11.1 (Lim Kinases); EC 2.7.11.1 ( ... is a highly conserved actin-binding protein across all eukaryotes and is involved in numerous actin-based processes by ... The cytokine leukemia inhibitory factor (LIF) is essential for rendering the uterus receptive for blastocyst implantation. In ... accelerating Cofilin severing actin filament. However, the function and the mechanism of WDR1 in mammalian early development ...
  • 1995 ). It was also shown that Arabidopsis thaliana ADF1 (AtADF1) increases assembly of F-actin at higher concentration (Carlier et al. (springer.com)
  • The Pseudomonas syringae type III effector HopG1 induces actin filament remodeling in Arabidopsis in association with disease symptom development. (msu.edu)
  • As part of an HHMI funded research project, I showed that overexpression (OE) of actin (ACT2) in Arabidopsis thaliana alters the expression of genes involved in plant immunity. (oregonstate.edu)
  • Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. (rcsb.org)
  • We have discussed the structure, the function and the stability of the protein and the way it is regulated in different actin-mediated cellular processes to control the machinery of actin polymerization. (springer.com)
  • The actin depolymerizing factors (ADFs) play important roles in several cellular processes that require cytoskeletal rearrangements, such as cell migration, but little is known about the in vivo functions of ADFs in developmental events like branching morphogenesis. (prolekare.cz)
  • We are now working to define 1) the basal function of these specific effector targets/processes, and 2) the impact of pathogen targeting on the disruption of homeostatic cellular processes requiring actin. (msu.edu)
  • Controlled actin assembly is crucial to a wide variety of cellular processes, including polarity establishment during early development. (biologists.org)
  • These calcium-dependent actin rearrangements induced by intracellular NSP4 expression may contribute to rotavirus pathogenesis by interfering with cellular processes dependent on subcortical actin remodeling, including ion transport and viral release. (asm.org)
  • The elicitor-responsive gene for a GRAS family protein, CIGR2, suppresses cell death in rice inoculated with rice blast fungus via activation of a heat shock transcription factor, Os Hsf23. (msu.edu)
  • Comparison of expression Quantitative Trait Loci (eQTL) between treatments revealed an inoculation-dependent expression polymorphism implicating Actin depolymerizing factor3 (within the Rpg-TTKSK locus) as a candidate susceptibility gene. (nih.gov)
  • Others have previously shown that knockout (KO) mutants of actin depolymerizing factor 4 are affected in the same gene as ACT2-OE. (oregonstate.edu)
  • The invasive stages of Toxoplasma gondii , an Apicomplexan parasite, actively invade their host cells in an actin-dependent way. (pnas.org)
  • Actin and myosin have been localized by immunoelectron microscopy to the apical end of the parasite and in the space between the plasma membrane and the outer face of the inner membrane complex (IMC) in both Toxoplasma and in Plasmodium falciparum merozoites ( 10 - 14 ). (pnas.org)
  • In fact, recent evidence from Toxoplasma implies that most of the cellular actin is sequestered as monomeric G-actin ( 9 ). (pnas.org)
  • Our results define the conoid and apical complex as a major site of actin polymerization in Toxoplasma, consistent with the role of the apical end in host-cell invasion and polarized secretion. (pnas.org)
  • abstract = "Actin dynamics determines podocyte morphology during development and in response to podocyte injury and might be necessary for maintaining normal podocyte morphology. (elsevier.com)
  • Actin fibers readily come apart (sever) and join back together, depending on the needs of the cell. (plantae.org)
  • The ADFs were divided into two categories based on activity: 1) D-type ( d epolymerizing F-actin) ADFs, which sever or depolymerize F-actin and 2) B-type ( b undling F-actin) ADFs, which bind to and bundle F-actin. (plantae.org)
  • Together, these results suggest that Shank3 deficiency induces NMDAR hypofunction by interfering with the Rac1/PAK/cofilin/actin signaling, leading to the loss of NMDAR membrane delivery or stability. (jneurosci.org)
  • Active cofilin could advance phagocytosis by promoting F-actin remodeling, which supports the production of membrane protrusions (e.g., filopodia), which, as we also revealed, are instrumental in myelin phagocytosis. (biomedcentral.com)
  • The terminal branches of these actin-rich membrane extensions, called foot processes, interdigitate with each other, forming specialized intercellular junctions called slit diaphragms. (asm.org)
  • Growth factor receptor-bound protein 2 (Grb2) has been proposed to play important roles in the membrane localization and activation of Vav through dimerization of its C-terminal Srchomology 3 (SH3) domain (GrbS) and the N-terminal SH3 domain of Vav (VavS). (nii.ac.jp)
  • Ellis S and Mellor H (2000) The novel Rho‐family GTPase rif regulates coordinated actin‐based membrane rearrangements. (els.net)
  • 1993 ). Biochemical characterization of plant ADF was first performed with Zea mays ADF3 (ZmABP3 then renamed as ZmADF3), confirming its conserved activity to bind both F- and G-actin (Rozycka et al. (springer.com)
  • The amino terminal CH domain has the intrinsic ability to bind actin, albeit with lower affinity than the complete ABD, whereas the carboxy terminal CH bind actin extremely weakly or not at all. (embl.de)
  • Although these studies suggest that Arp2/3 complex induces formation of the branched actin network in the bulbous spine head, experimental evidence is still lacking. (rupress.org)
  • When expressed in cultured cells, wild-type DLIMK, but not its kinase-inactive form, induces changes in actin cytoskeletal organization. (sdbonline.org)
  • The small GTPase Rif and its effector mDia2 formin play a central role in regulating actin dynamics during filopodia elongation. (rupress.org)
  • Kusano K, Abe H, Obinata T (1999) Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin. (springer.com)
  • However, the intermonomer interactions that stabilize F-actin have not been elucidated because of a lack of an F-actin crystal structure. (biomedsearch.com)