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.

Vertebrate isoforms of actin capping protein beta have distinct functions In vivo. (1/91)

Actin capping protein (CP) binds barbed ends of actin filaments to regulate actin assembly. CP is an alpha/beta heterodimer. Vertebrates have conserved isoforms of each subunit. Muscle cells contain two beta isoforms. beta1 is at the Z-line; beta2 is at the intercalated disc and cell periphery in general. To investigate the functions of the isoforms, we replaced one isoform with another using expression in hearts of transgenic mice. Mice expressing beta2 had a severe phenotype with juvenile lethality. Myofibril architecture was severely disrupted. The beta2 did not localize to the Z-line. Therefore, beta1 has a distinct function that includes interactions at the Z-line. Mice expressing beta1 showed altered morphology of the intercalated disc, without the lethality or myofibril disruption of the beta2-expressing mice. The in vivo function of CP is presumed to involve binding barbed ends of actin filaments. To test this hypothesis, we expressed a beta1 mutant that poorly binds actin. These mice showed both myofibril disruption and intercalated disc remodeling, as predicted. Therefore, CPbeta1 and CPbeta2 each have a distinct function that cannot be provided by the other isoform. CPbeta1 attaches actin filaments to the Z-line, and CPbeta2 organizes the actin at the intercalated discs.  (+info)

Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments. (2/91)

Toxoplasma gondii relies on its actin cytoskeleton to glide and enter its host cell. However, T. gondii tachyzoites are known to display a strikingly low amount of actin filaments, which suggests that sequestration of actin monomers could play a key role in parasite actin dynamics. We isolated a 27-kDa tachyzoite protein on the basis of its ability to bind muscle G-actin and demonstrated that it interacts with parasite G-actin. Cloning and sequence analysis of the gene coding for this protein, which we named Toxofilin, showed that it is a novel actin-binding protein. In in vitro assays, Toxofilin not only bound to G-actin and inhibited actin polymerization as an actin-sequestering protein but also slowed down F-actin disassembly through a filament end capping activity. In addition, when green fluorescent protein-tagged Toxofilin was overexpressed in mammalian nonmuscle cells, the dynamics of actin stress fibers was drastically impaired, whereas green fluorescent protein-Toxofilin copurified with G-actin. Finally, in motile parasites, during gliding or host cell entry, Toxofilin was localized in the entire cytoplasm, including the rear end of the parasite, whereas in intracellular tachyzoites, especially before they exit from the parasitophorous vacuole of their host cell, Toxofilin was found to be restricted to the apical end.  (+info)

Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin. (3/91)

Actin polymerization in Apicomplexa protozoa is central to parasite motility and host cell invasion. Toxofilin has been characterized as a protein that sequesters actin monomers and caps actin filaments in Toxoplasma gondii. Herein, we show that Toxofilin properties in vivo as in vitro depend on its phosphorylation. We identify a novel parasitic type 2C phosphatase that binds the Toxofilin/G-actin complex and a casein kinase II-like activity in the cytosol, both of which modulate the phosphorylation status of Toxofilin serine53. The interplay of these two molecules controls Toxofilin binding of G-actin as well as actin dynamics in vivo. Such functional interactions should play a major role in actin sequestration, a central feature of actin dynamics in Apicomplexa that underlies the spectacular speed and nature of parasite gliding motility.  (+info)

Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance. (4/91)

The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP alpha and beta subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The alpha COOH-terminal region was more important than that of beta. The significance of CP's actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.  (+info)

ASP-56, a new actin sequestering protein from pig platelets with homology to CAP, an adenylate cyclase-associated protein from yeast. (5/91)

A new 56 kDa actin-binding protein (ASP-56) was isolated from pig platelet lysate. In falling ball viscosimetry it caused a reduction in viscosity that could be attributed to a decrease in the concentration of polymeric actin. Fluorescence measurements with NBD-labelled actin showed reduction of polymeric actin, too. These results could be explained by sequestering of actin in a non-polymerizable 1:1 ASP-56/actin complex. Sequencing of about 20 tryptic peptides of ASP-56 and comparison with known sequences revealed about 60% homology to the adenylate cyclase-associated protein (CAP) from yeast.  (+info)

The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein. (6/91)

CKIP-1 is a pleckstrin homology domain-containing protein that interacts with protein kinase CK2. To elucidate the functions of CKIP-1, we generated human osteosarcoma cell lines with tetracycline-regulated expression of Flag-CKIP-1. Flag-CKIP-1 expression resulted in distinct changes in cellular morphology. Therefore, we examined the actin profile by immunofluorescence, quantitative measurement of phalloidin binding, and immunoblot analysis. These studies demonstrate that Flag-CKIP-1 expression resulted in increases in F-actin staining and protein levels of beta-actin. To elucidate the mechanisms behind the observed phenotype, we utilized tandem affinity purification to isolate CKIP-1 interacting proteins. Mass spectrometry analysis led to the identification of the actin capping protein subunits, CPalpha and CPbeta, as novel CKIP-1 interaction partners. Interactions were confirmed by coimmunoprecipitation and by colocalization. Furthermore, we demonstrate that Ser9 of CPalpha is phosphorylated by protein kinase CK2 in vitro, that CPalpha is phosphorylated in vivo, and that treatment with a CK2-specific inhibitor results in a decrease in CPalpha phosphorylation. Finally, we demonstrate that CKIP-1 and CK2 inhibit the activity of actin capping protein at the barbed ends of actin filaments. Overall, our results are consistent with CKIP-1 playing a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein.  (+info)

Mutations in the Drosophila orthologs of the F-actin capping protein alpha- and beta-subunits cause actin accumulation and subsequent retinal degeneration. (7/91)

The progression of several human neurodegenerative diseases is characterized by the appearance of intracellular inclusions or cytoskeletal abnormalities. An important question is whether these abnormalities actually contribute to the degenerative process or whether they are merely manifestations of cells that are already destined for degeneration. We have conducted a large screen in Drosophila for mutations that alter the growth or differentiation of cells during eye development. We have used mitotic recombination to generate patches of homozygous mutant cells. In our entire screen, mutations in only two different loci, burned (bnd) and scorched (scrd), resulted in eyes in which the mutant patches appeared black and the mutant tissue appeared to have undergone degeneration. In larval imaginal discs, growth and cell fate specification occur normally in mutant cells, but there is an accumulation of F-actin. Mutant cells degenerate much later during the pupal phase of development. burned mutations are allelic to mutations in the previously described cpb locus that encodes the beta-subunit of the F-actin capping protein, while scorched mutations disrupt the gene encoding its alpha-subunit (cpa). The alpha/beta-heterodimer caps the barbed ends of an actin filament and restricts its growth. In its absence, cells progressively accumulate actin filaments and eventually die. A possible role for their human orthologs in neurodegenerative disease merits further investigation.  (+info)

A modular design for the clathrin- and actin-mediated endocytosis machinery. (8/91)

Endocytosis depends on an extensive network of interacting proteins that execute a series of distinct subprocesses. Previously, we used live-cell imaging of six budding-yeast proteins to define a pathway for association of receptors, adaptors, and actin during endocytic internalization. Here, we analyzed the effects of 61 deletion mutants on the dynamics of this pathway, revealing functions for 15 proteins, and we analyzed the dynamics of 8 of these proteins. Our studies provide evidence for four protein modules that cooperate to drive coat formation, membrane invagination, actin-meshwork assembly, and vesicle scission during clathrin/actin-mediated endocytosis. We found that clathrin facilitates the initiation of endocytic-site assembly but is not needed for membrane invagination or vesicle formation. Finally, we present evidence that the actin-meshwork assembly that drives membrane invagination is nucleated proximally to the plasma membrane, opposite to the orientation observed for previously studied actin-assembly-driven motility processes.  (+info)

Toxoplasma, a human pathogen and a model apicomplexan parasite, actively and rapidly invades host cells. To initiate invasion, the parasite induces the formation of a parasite-cell junction, progressively propels itself through the junction inside a newly formed vacuole that encloses the entering parasite. Litle is known how a few micron-large diameter parasite overcome the host cell cortical actin barrier to support these remarkably rapid process of internalization (, few seconds). Correlative light and electron microscopy in conjunction with electron tomography and three-dimensional image analysis indicate that toxofilin an actin-binding protein, secreted by invading parasites correlates with localized sites of disassembly of the host cell actin meshwork. Moreover, quantitative fluorescence speckle microscopy in cells expressing toxofilin indicates that toxofilin regulates actin filament disassembly and turnover. Furthermore, Toxoplasma tachyzoites lacking toxofilin, are impaired in cortical ...
Toxoplasma gondii, the protozoan parasite that causes toxoplasmosis, initiates invasion of its host cells by inducing the assembly of a parasite-cell junction. Concomitantly, the plasma membrane of the host cell invaginates around the parasite to form a parasitophorous vacuole (PV). The parasite then propels itself through the junction and multiplies in its host cell within the PV. Given the size of the parasite, PV formation and parasite internalization are likely to require local loosening of the host cell cortical actin barrier, but how is this achieved? On page 4333, Isabelle Tardieux, colleagues and collaborators propose that toxofilin, an actin binding protein secreted by T. gondii, facilitates parasite invasion by regulating host cortical actin filament turnover. They show that parasites lacking toxofilin are impaired in cell invasion, although they eventually enter host cells, and that toxofilin secreted by invading parasites specifically associates with areas of host cell actin meshwork ...
In the present study, we demonstrated the prognostic value of CapG as well as its important role in proliferation and metastasis of glioma. In the TCGA data analysis, we attempted to explore the correlation of CapG with common genetic alterations of GBM. Notably, we noted that CapG expression was correlated to several of them (amplifications of CDK6, EGFR, MET and SYK, mutations of PTEN and RB1), and the correlation was only observed in non-proneural or proneural subtype. These data provide a clue for further study of the regulation of CapG expression in GBM patients. Moreover, we investigated the influence of differential CapG expression on GBM patient prognosis stratified by these molecular alterations. Kaplan-Meier analysis suggested that the prognostic significance of CapG was dependent on the status of EGFR or CDK6 alteration.. EGFR is a vital oncogene found in many malignancies, and the majority of GBM show activated EGFR signaling through its amplification or genetic alteration, which ...
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. The isoform beta-3 may play a role in spermatogenesis. Alternatively, may play a role in later maturation steps such as capacitation and fertilization which involve changes of membrane domains. May play a role in the regulation of cell morphology and cytoskeletal organization.
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Looking for info on why my daughter who has CP has suddenly developed a twitching of her arm. It is pretty severe. The arm constantly moves back and f
Expression of CARMIL1 (CARMIL, dJ501N12.1, FLJ20048, LRRC16, LRRC16A) in cervix, uterine tissue. Antibody staining with HPA029038 and HPA029039 in immunohistochemistry.
TY - JOUR. T1 - Listerias right-handed helical rocket-tail trajectories. T2 - Mechanistic implications for force generation in actin-based motility. AU - Zeile, William L.. AU - Zhang, Fangliang. AU - Dickinson, Richard B.. AU - Purich, Daniel L.. PY - 2005/2/1. Y1 - 2005/2/1. N2 - Listeria monocytogenes forms right-handed helical rocket tail trajectories during actin-based motility in cell-free extracts, and this stereochemical feature is consistent with actoclampins affinity-modulated, clamped-filament elongation model [Dickinson and Purich, 2002: Biophys J 82:605-617]. In that mechanism, right-handed torque is generated by an end-tracking molecular motor, each comprised of a filament barbed end and clamping protein that processively traces the right-handed helix of its filament partner. By contrast, torque is not a predicted property of those models (e.g., elastic propulsion, elastic Brownian ratchet, tethered ratchet, and insertional polymerization models) requiring filament barbed ends to ...
Looking for online definition of barbed end in the Medical Dictionary? barbed end explanation free. What is barbed end? Meaning of barbed end medical term. What does barbed end mean?
When the heavier homologues KSCN and KSeCN are employed, the Fe(III) compounds 3 and 4 are isolated in low yield (Scheme 1). The formation of these compounds is unexpected, since generally no redox processes are encountered when pseudohalides coordinate to transition metals,15 which implies that the Cp′Fe-fragment is susceptible to redox chemistry. Furthermore, this redox behavior is apparently facilitated by the synergy between two or more Fe atoms, an effect that also accounts for the facile N2 release from [Bu4N]N3 in the presence of [(tbsL)Fe3(thf)].4 Furthermore, S-C bond cleavage of a SCN− ligand is a rare event, but has previously been observed in [Pd3(SCN)(μ3-CO)(μ-dppm)3]+ to form [Pd3(μ3-S)(CN)(μ-dppm)3]+.16 The FeMoco nitrogenase enzyme also transiently binds SCN− before reduction to HCN and H2S occurs; but the mechanism of this biological SCN− reduction remains unknown.17 Cleavage of the S-C and Se-C bond to form 3 and 4 requires that the Fe(II) atoms are oxidized to ...
Expression of CARMIL1 (CARMIL, dJ501N12.1, FLJ20048, LRRC16, LRRC16A) in endometrium 2 tissue. Antibody staining with HPA029038 and HPA029039 in immunohistochemistry.
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Actin cytoskeleton dynamics play vital roles in most forms of intracellular trafficking by promoting the biogenesis and transport of vesicular cargoes. Mounting evidence indicates that actin dynamics and membrane-cytoskeleton scaffolds also have essential roles in macroautophagy, the process by whic …
On Fri, Feb 21, 2003 at 01:11:58PM +0100, Maciej W. Rozycki wrote: , , , Does Cobalt have a processor that implements its pipeline differently or , , , interlocks on CP0 loads? If not, Ill apply the following fix. , , , , Mfc0 doesnt need a nops on any R4000 class CPU I know of. , , Well, my MIPS R4k manual is vague on this matter and my IDT software , manual for R3k, R4k, R5k is even explicit on the load delay slot of mfc0. , But a run-time test proves otherwise. , , I stand corrected then unless someone finds a counter-example. All I can say its working fine like this since 1984 for R4000 class CPUs. Ralf ...
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海词词典,最权威的学习词典,专业出版actin是什么意思,actin的用法,actin翻译和读音等详细讲解。海词词典:学习变容易,记忆很深刻。
What is Actin ransomware? And how does it execute its attack? Actin ransomware is a dangerous threat and is a new variant of Phobos ransomware. This crypto-virus was discovered at the end of May 2019. It appends the ...Actin extension to its targeted files. The moment it enters a system, this crypto-malware performs
Inspite of the fact that many cant get over the Ghostface Killah influence in Action Bransons flow, he remains to … More. ...
ஆக்டின் என்பது தசை செல்களில் உள்ள நாராலான ஒரு புரத வகையாகும்.. ...
Actin filament elongation as a function of the surface density of side-binding proteins.(A-B) The change in length, ΔL, as a function of time for a filament
The effect of applying an external load to actin filaments moving in the in vitro motility assay is studied. Bead-tailed actin filaments were made by polym
This study addresses three coach behaviours effects (warmness behaviour (WB); stimulating action (SA) and planning and structuring activities (PSA)) in two dimensions of coaching outcomes (coachees performance (CP) and the quality of the coach-coachee relationship (QCCR)). The paper argues that coaching is a helpful tool to achieve greater performances in the long run when considering coaches who present higher levels of maturity. Results reveal the positive impact of SA and PSA over CP and QCCR. The adoption of WB has a negative impact on CP and a positive impact on the QCCR. Evidence also supports the relevancy of coaching experience over coaching training. Such results pose a paradox worth exploring in subsequent studies, for it challenges the usefulness of coaches training. Contributions are related to introducing the concept of WB within the organisational context and addressing two different time horizons regarding the coach behaviour. ...
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Intentionally slow lifting is believed by some to be the best way to develop strength. Learn the truth behind the myth about the force-velocity relationship.
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Cytoskeleton, Inc provides fluorescent Spirochrome SPY555-actin live cell imaging probe to label actin for single or dual fluorescent color imaging and is an improvement over Syto61, DRAQ5, or Vybrant DyeCycle Ruby dyes.
Actin (pan alpha), 0.1 mg. Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Figure 1 Tying a knot in an actin filament. Explanatory drawings are added in images 3 7. In images 3 and 7, the microscope focus was moved to below the filament to bring down the end beads which were trapped at the focus level; the focus was above the filament in image 5. Scale bar, 10 µm. ...
Maréchal, Georges ; Beckersbleukx, G.. [Effects of nitric oxide on force-velocity relationship of striated skeletal musculature of the mouse].64th Conference of the Societe-de-Physiologie (LILLE(France), Sep 18-20, 1996). In: Archives of Physiology and Biochemistry : the journal of metabolic diseases, Vol. 104, no. 4, p. D72 (1996 ...
End capping of cytoskeletal filaments is a key mechanism for regulating filaments elongation and disassembly, as well as the organization of the cytoskeletal architecture. CP binds to the barbed ends of actin filaments to inhibit further elongation and is involved in the formation of branched actin networks in concert with Arp2/3 (Akin and Mullins, 2008). Here, we show that CP plays an essential role in the formation of dendritic spines. In particular, CP knockdown promoted the formation of thin filopodia-like protrusions and inhibited proper spine development. Dendritic spines initiate as filopodia-like protrusions from dendritic shafts, and then convert to mature spine structure with an expanded head (Ziv and Smith, 1996; Yoshihara et al., 2009; Hotulainen and Hoogenraad, 2010). Our data thus suggest that CP may function in the transition of filopodia to spines. CP is known to function in the formation of branched actin networks in lamellipodia in non-neuronal cells, and CP knockdown promotes ...
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.. ...
Treatment with SMIFH2 decreases the actin level in oocytes and impairs spindle formation.A. Treatment with SMIFH2 decreases the cortical actin level in maturing
Dynamic behavior of actin filaments in cells is the basis of many different cellular activities. Remodeling of the actin filament network involves polymerization and depolymerization of the filaments. Proteins that regulate these behaviors include proteins that sever and/or cap actin filaments. This report presents direct observation of severing of fluorescently-labeled actin filaments. Coverslips coated with gelsolin, a multi-domain, calcium-dependent capping and severing protein, bound rhodamine-phalloidin-saturated filaments along their length in the presence of EGTA. Upon addition of calcium, attached filaments bent as they broke. Actophorin, a low molecular weight, monomer sequestering, calcium-independent severing protein did not sever phalloidin-saturated filaments. Both gCap 39, a gelsolin-like, calcium-dependent capping protein that does not sever filaments, and CapZ, a heterodimeric, non-calcium-dependent capping protein, bound the filaments by one end to the coverslip. Visualization ...
Cell behavior is controlled by extracellular signals that work through signal transduction pathways to regulate the organization of the actin cytoskeleton. Some of these extrinsic signals positively affect the cytoskeleton and induce actin polymerization, but extrinsic signals that negatively regulate and disassemble actin filaments also exist. A family of multidomain proteins, the MICALs, directly associates with Semaphorins, cell surface receptors involved in negative or repulsive cues. Working with purified proteins and in vivo, Hung et al. now find that actin filaments serve as a direct substrate for Micals enzymatic activity. Mical posttranslationally alters actin at its methionine 44 residue, which disrupts the association between actin monomers and cutting actin filaments. Altering the methionine 44 residue makes actin resistant to Mical-mediated disassembly in vitro and in vivo in Drosophila.. R.-J. Hung, C. W. Pak, J. R. Terman, Direct redox regulation of F-actin assembly and ...
0062] In some implementations, as illustrated by FIG. 4, a needle 122a can include a barbed end 146 defining a recessed engagement surface 148. The needle capture device can comprise a needle attachment fitting or cuff 136. Specifically, the needle attachment cuff 136 can have a roughly cylindrical shape and include an axial channel 150 configured to receive the barbed end 146 of needle 122a therein. In additional implementations, the needle attachment cuff 136 can include shapes other than cylindrical ones, such as, for example, conical. The needle attachment cuff 136 can include one or more features configured to lock the barbed end 146 of the needle 122a therein. For instance, as shown in FIG. 4, the needle attachment cuff 136 can include at least one tab 152. The tab 152 may be mechanically formed to be smaller than the diameter of surface 148. The tab 152 can be resiliently biased into channel 150. As the needle 122a advances into the needle attachment cuff 136, the barbed end 146 can ...
misc{2054071, author = {Tondeleir, Davina and Ampe, Christophe and Vandekerckhove, Jo{\e}l}, language = {eng}, publisher = {Wiley}, series = {Encyclopedia of life sciences}, title = {Actin and actin filaments}, url = {http://dx.doi.org/10.1002/9780470015902.a0001255.pub3}, year = {2011 ...
GO:0030833. Any process that modulates the frequency, rate or extent of the assembly of actin filaments by the addition of actin monomers to a filament. ...
Fav-store specialize in supplying special featured herbal medecines, developed to improve your life and makes better your health. We present a 60 day full money back guarantee. Actin one creamNOTORIOUS B.I.G. LYRICS - Big Poppa - A-Z Lyrics.
As of March 2017, during the lab retreat, the group is composed of Guillaume, Sandy, Yan, Emiko, Héliciane, Bérengère, Hugo, Antoine and Mikaël. ...
Branched actin networks harness the free energy of actin filament assembly to generate forces required for many important cellular processes (Pollard & Cooper, 2009; Blanchoin et al, 2014). These self‐assembling, cytoskeletal structures push against loads (generally cellular membranes) by promoting nucleation and elongation of actin filaments near the load surface (Pollard et al, 2000). Filament nucleation in branched networks is controlled by membrane‐associated signaling molecules, which recruit nucleation‐promoting factors (NPFs) that, in turn, localize the Arp2/3 complex and stimulate its actin nucleation activity (Pollard et al, 2000; Rotty et al, 2013). Filament elongation near the membrane surface is generally assumed to occur via diffusion‐limited incorporation of actin monomers directly from solution (Pollard et al, 2000), with possible assistance from membrane‐associated actin polymerases, such as formins and Ena/VASP proteins (Dominguez, 2009). The fact that neither formins ...
TY - JOUR. T1 - Actin Filament Bundling and Different Nucleating Effects of Mouse Diaphanous-Related Formin FH2 Domains on Actin/ADF and Actin/Cofilin Complexes. AU - Machaidze, Gia. AU - Sokoll, Andrea. AU - Shimada, Atsushi. AU - Lustig, Ariel. AU - Mazur, Antonina. AU - Wittinghofer, Alfred. AU - Aebi, Ueli. AU - Mannherz, Hans Georg. PY - 2010/11/5. Y1 - 2010/11/5. N2 - Mouse Diaphanous-related formins (mDias) are members of the formin protein family that nucleate actin polymerization and subsequently promote filamentous actin (F-actin) elongation by monomer addition to fast-growing barbed ends. It has been suggested that mDias preferentially recruit actin complexed to profilin due to their proline-rich FH1 domains. During filament elongation, dimeric mDias remain attached to the barbed ends by their FH2 domains, which form an anti-parallel ring-like structure enclosing the filament barbed ends. Dimer formation of mDia-FH2 domains is dependent on their N-terminal lasso and linker subdomains ...
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 ...
I have to do a literature review on a topic involving neurophysiology. So I chose to pick one about the force-velocity relationship of muscle contractions. The relationship shows that as muscle velocity increases, muscle force decreases. I was wondering if anybody has any research articles that show the opposite: That as velocity increases muscle force increases as well. I have searched to no avail. I appreciate any help.
The polymerization of scallop p-like actin is significantly slower than that of skeletal muscle alpha-actin. To reveal which steps of polymerization contribute to this difference, we estimated the efficiency of nucleation of the two actins, the rates of filament elongation at spontaneous and gelsolin-nucleated polymerization and the turnover rates of the filament Subunits at steady-state. Scallop actin nucleated nearly twice less efficient than rabbit actin. In actin filaments with free ends, when dynamics at the barbed ends overrides that at the pointed ends, the relative association rate constants of alpha- and beta-actin were similar, whereas the relative dissociation rate constant of beta-ATP-actin subunits was 2- to 3-fold higher than that of alpha-actin. The 2- to 3-fold faster polymerization of skeletal muscle versus scallop Ca-actin was preserved with gelsolin-capped actin filaments when only polymerization at the pointed end is possible. With gelsolin-induced polymerization, the rate ...
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
It is generally accepted that cytochalasin B (CB), as well as other cytochalasins, shorten actin filaments by blocking monomer addition at the fast-growing (barbed) end of these polymers. Despite the predominance of this mechanism, recent evidence suggests that other interactions may also occur be …
Encyclopedia. Several years ago I had jotted down some interesting points about the Great Egyptian Revolt of the mid-Ptolemaic era, as it was something I had only recently discovered even existed after reading through some lecture notes of Willy Clarisse published online. I pulled them together into a fairly good (IMHO, and definitely bloody good by CP standards) article and put it on CP, and thought little more of it. It was so far of the assflys radar it escaped the molestations of Ed Poor or t3h crazy of Kendoll for ages. Then my old laptop was stolen. Most of my stuff I had copies of on my partners one for safekeeping, so I didnt worry. So, a few days ago, I was mulling over a mid-semester essay I need to summon up, and decided to dig up the old article and use it (and the Bibliography) as the rough core to build an assignment around. Not backed up. No worries! I can pull up the old CP article, as that had most of the material in it, and its only fact checking and biblio anyway. ...
TABLE-US-00018 TABLE 15 Diagnostic Genetic Probes and Amplimers for the Candidate Mahidol DEN-1, DEN-2, DEN-3, and DEN-4 Vaccine Viruses. Genetic Locus Primer Designation SEQ ID NO: D1V-1323 Probe pcD1V-1308 44 F fD1V-1298 45 R rD41V-1347 46 D1V-1541, 1543, 1545 Probe pcD1V-1530 47 F fD1V-1519 48 R rD1V-1567 43 D1V-1567 Probe pD1V-1580 50 F fD1V-1545 51 R rD1V-1608 52 D1V-1608 Probe pcD1V-1595 53 F fD1V-1567 54 R rD1V-1626 55 D1V-2363 Probe pD1V-2374 56 F fD1V-2334 57 R rD1V-2386 58 D1V-2695 Probe pcD1V-2686 59 F fD1V-2660 60 R rD1V-2735 61 D1V-2782 Probe pDIV-2767 62 F fD1V-2752 63 R rD1V-2801 64 D1V-5063 Probe pcD1V-5052 65 F fD1V-5040 66 R rD1V-5095 67 D1V-6048 Probe pD1V-6059 68 F fD1V-6030 69 R rD1V-6069 70 D1V-6806 Probe pcD1V-6793 71 F fD1V-6780 72 R rD1V-6825 73 D1V-7330 Probe pD1V-7343 74 F fD1V-7310 75 R rD1V-7351 76 D1V-9445 Probe pcD1V-9433 77 F fD1V-9419 78 R rD1V-9485 79 D2V-57 Probe pD2V-69 80 F fD2V-32 81 R rD2V-81 82 D2V-524 Probe pcD2V-513 83 F fD2V-492 84 R rD2V-551 85 ...
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. ...
Filament formation is required for most of the functions of actin. However, the intermonomer interactions that stabilize F-actin have not been elucidated because of a lack of an F-actin crystal structure. The Holmes muscle actin model suggests that a
F-actin capping protein. FNDC38 - Represses transcription. Tumour metastasis. Raldh2/aldh1a2 - Represses transcription. ...
"Mammalian CARMIL Inhibits Actin Filament Capping by Capping Protein". Developmental Cell. 9 (2): 209-221. doi:10.1016/j.devcel. ... Leucine rich repeat containing 16A is a protein that in humans is encoded by the LRRC16A gene. The gene is also known as LRRC16 ...
In the proposed 'capping' model, an uncharacterized protein complex moves rearward, moving the parasites forward. The ... This is accomplished through the use of an actin and myosin complex. The complexes require an actin cytoskeleton to perform ... Both protists use protein complexes similar to those that are formed by the gregarines for gliding motility and invading target ... doi:10.1111/j.1550-7408.1979.tb04197.x. Heintzelman MB (June 2004). "Actin and myosin in Gregarina polymorpha". Cell Motil. ...
2005). "Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins". J. Biol. Chem. 280 (31 ... 2006). "Spectrin interacts with EVL (Enabled/vasodilator-stimulated phosphoprotein-like protein), a protein involved in actin ... 2000). "Fyn-binding protein (Fyb)/SLP-76-associated protein (SLAP), Ena/vasodilator-stimulated phosphoprotein (VASP) proteins ... Ena/VASP-like protein is a member of the Ena/VASP family of proteins that in humans is encoded by the EVL gene. GRCh38: Ensembl ...
Actin-related protein 2/3 complex subunit 1A is a protein that in humans is encoded by the ARPC1A gene. This gene encodes one ... Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with ... "Entrez Gene: ARPC1A actin related protein 2/3 complex, subunit 1A, 41kDa". Human ARPC1A genome location and ARPC1A gene details ... 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of ...
The encoded protein caps the pointed end of actin filaments preventing both elongation and depolymerization. The capping ... This gene encodes a muscle-specific member of the tropomodulin family of actin-regulatory proteins. ... that caps actin filament pointed ends in fast skeletal muscle". J. Biol. Chem. 274 (40): 28466-75. doi:10.1074/jbc.274.40.28466 ... Tropomodulin 4 (muscle) also known as TMOD4 is a protein which in humans is encoded by the TMOD4 gene. ...
The encoded protein caps the pointed end of actin filaments preventing both elongation and depolymerization. The capping ... This gene encodes a neuronal-specific member of the tropomodulin family of actin-regulatory proteins. ... Tropomodulin 2 (neuronal) also known as TMOD2 is a protein which in humans is encoded by the TMOD2 gene. ... a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin". J. Cell Sci. 109 (9): 2299-310. ...
... A1 CAPZA2 CAPZA3 CAPZB CapZ Actin Capping Protein at the US National Library of Medicine Medical Subject Headings (MeSH) ... Heiss, Steven; Cooper, John (June 24, 1991). "Regulation of CapZ, an actin capping protein of chicken muscle, by anionic ... Gremm, D.; Wegner, A. (2000-07-01). "Gelsolin as a calcium-regulated actin filament-capping protein". European Journal of ... The activity regulation of this protein can be done by other regulatory proteins that bind to the actin filaments blocking the ...
This, along with plus end capping proteins, such as capZ stabilise the structure of the actin filament. End capping is ... is a protein which binds and caps the minus end of actin (the "pointed" end), regulating the length of actin filaments in ... The protein functions by physically blocking the spontaneous dissociation of ADP-bound actin monomers from the minus end of the ... TMOD1 TMOD2 TMOD3 TMOD4 Rao, J. N.; Madasu, Y.; Dominguez, R. (24 July 2014). "Mechanism of actin filament pointed-end capping ...
"Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila". Development. 138 (11): 2337-2346 ... shown that one of the proteins that regulates the skeleton of the cell also acts to block activation of genes that promote cell ... protein structure and design, synthesis and theory of chemicals with biological interest, molecular microbiology, plant ...
However, the protein appears to be able to interact with adenylyl cyclase-associated protein and actin. CAP2 has been shown to ... Hubberstey A, Yu G, Loewith R, Lakusta C, Young D (Jun 1996). "Mammalian CAP interacts with CAP, CAP2, and actin". Journal of ... "Entrez Gene: CAP2 CAP, adenylate cyclase-associated protein, 2 (yeast)". Human CAP2 genome location and CAP2 gene details page ... "Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins". Journal of Cell Science. 107 (6 ...
The protein binds to actin monomers and filaments, G actin and F actin, respectively. Cofilin causes depolymerization at the ... Cofilin/ADF(destrin) is likely to sever F-actin without capping and prefers ADP-actin. These monomers can be recycled by ... ATP-actin is then available for assembly. Cofilin binds monomeric (G-actin) and filamentous actin (F-actin). Its binding ... also known as ADF or actin depolymerizing factor Actin-binding proteins regulate assembly and disassembly of actin filaments. ...
The human protein is able to interact with other molecules of the same protein, as well as with CAP2 and actin. CAP1 has been ... The protein encoded by this gene is related to the S. cerevisiae CAP protein, which is involved in the cyclic AMP pathway. ... Hubberstey A, Yu G, Loewith R, Lakusta C, Young D (Apr 1997). "Mammalian CAP interacts with CAP, CAP2, and actin". J Cell ... "Mammalian CAP interacts with CAP, CAP2, and actin". J. Cell. Biochem. UNITED STATES. 61 (3): 459-66. doi:10.1002/(SICI)1097- ...
Abl is also thought to promote repulsive signaling by binding to adenylyl cyclase associated proteins (CAP), which regulate ... a Rho GTPase which mediates actin depolymerization. In Drosophila, the SH3-SH2 adaptor protein Dock binds directly to the CC2 ... Another protein Commissureless (Comm) was found to be an essential regulator of Robo: in comm mutants, Robo activity is too ... Brose K, Bland KS, Wang KH, Arnott D, Henzel W, Goodman CS, Tessier-Lavigne M, Kidd T (March 1999). "Slit proteins bind Robo ...
2007). "The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein". J. Biol. Chem. 281 (47): ... CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein". Mol ... 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with ...
The protein regulates growth of the actin filament by capping the barbed end of growing actin filaments. CapZβ functions to cap ... F-actin-capping protein subunit beta, also known as CapZβ is a protein that in humans is encoded by the CAPZB gene. CapZβ ... Casella JF, Craig SW, Maack DJ, Brown AE (July 1987). "Cap Z(36/32), a barbed end actin-capping protein, is a component of the ... CAPZB is a member of the F-actin capping protein family. This gene encodes the beta subunit of the barbed-end actin binding ...
Further, Ena/VASP prevents the action of capping protein, which halts actin polymerization. Alberts, Bruce; Johnson, Alexander ... is a cytoskeletal protein actin projection on the leading edge of the cell. It contains a quasi-two-dimensional actin mesh; the ... Ena/VASP proteins are found at the leading edge of lamellipodia, where they promote actin polymerization necessary for ... The lamellipodium is born of actin nucleation in the plasma membrane of the cell and is the primary area of actin incorporation ...
"Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin ... A tropomyosin-binding protein". J Biol Chem. 267 (4): 2616-21. PMID 1370827. Sung LA, Fan Y, Lin CC (Dec 1996). "Gene ... Tropomodulin-1 is a protein that in humans is encoded by the TMOD1 gene. GRCh38: Ensembl release 89: ENSG00000136842 - Ensembl ... "Entrez Gene: TMOD1 tropomodulin 1". Ursitti JA, Fowler VM (1994). "Immunolocalization of tropomodulin, tropomyosin and actin in ...
Unphosphorylated Hsp27 has been shown to act as an actin capping protein, preventing actin reorganization and, consequently, ... Heat shock protein 27 (Hsp27) also known as heat shock protein beta-1 (HSPB1) is a protein that in humans is encoded by the ... Probably it functions as a mediator of solubility for hydrophobic sHsps and it stabilizes the protein and protein/substrate ... Fu L, Liang JJ (February 2002). "Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid ...
CAP/Ponsin protein, also known as Sorbin and SH3 domain-containing protein 1 is a protein that in humans is encoded by the ... multifunctional Src homology 3 domain-containing protein in formation of actin stress fibers and focal adhesions". The Journal ... CAP/Ponsin is part of an adaptor protein family, of which ArgBP2 and vinexin are also a part. These proteins contain a ... Nakayama M, Kikuno R, Ohara O (Nov 2002). "Protein-protein interactions between large proteins: two-hybrid screening using a ...
Actin polymerization together with capping proteins were recently used to control the 3-dimensional growth of protein filament ... including motor proteins, branching proteins, severing proteins, polymerization promoters, and capping proteins. Measuring ... Actin depolymerizing proteins such as ADF/cofilin. The actin filament network in non-muscle cells is highly dynamic. The actin ... Actin monomer-binding proteins profilin and thymosin β4 Filament barbed-end cappers such as Capping Protein and CapG, etc. ...
Additionally, they have been known to interact with the cytoskeleton adaptor protein, CAP/ponsin, suggesting cell signalling ... roles and regulation of actin organisation. Teneurin-3 regulates the structural and functional wiring of retinal ganglion cells ... Teneurins are transmembrane proteins. The name refers to "ten-a" (from "tenascin-like protein, accessory") and "neurons", the ... Ten-m refers to tenascin-like protein major are type II transmembrane glycoproteins. Teneurins are highly conserved between ...
"Actin capping protein: an essential element in protein kinase signaling to the myofilaments". Circulation Research. 90 (12): ... Actin-capping protein, CapZ appears to affect the localization of PKCε to Z-lines and modulates the cardiomyocyte response to ... Sarcomeric proteins have been identified in PKCε signaling complexes, including actin, cTnT, tropomyosin, desmin, and myosin ... Zeidman R, Trollér U, Raghunath A, Påhlman S, Larsson C (Jan 2002). "Protein kinase Cepsilon actin-binding site is important ...
... a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in ... Gelsolin, an actin filament severing protein, localizes at the tail of Listeria and accelerates the bacterium's motility. Once ... Smith, G. A.; Portnoy D. A. (July 1997). "Trends in Microbiology". How the Listeria monocytogenes ActA protein converts actin ... It induces directed polymerization of actin by the ActA transmembrane protein, thus pushing the bacterial cell around. L. ...
... that FH2 domains protect the rapidly elongating barbed ends of filaments from the vast molar excesses of actin capping proteins ... Profilin as a ubiquitous actin-binding protein is associated with most actin monomers in cells. Interactions between profilin- ... actin with the FH1 domain can accelerate the elongation at the FH2-capped barbed ends. The formin homology protein mDia1 is a ... "Formin leaky cap allows elongation in the presence of tight capping proteins". Curr. Biol. 13 (20): 1820-1823. doi:10.1016/j. ...
Calcium/calmodulin-regulated capping of the barbed ends of actin filaments". J. Biol. Chem. 271 (14): 7986-91. doi:10.1074/jbc. ... Alpha-adducin is a protein that in humans is encoded by the ADD1 gene. Adducins are a family of cytoskeleton proteins encoded ... Adducin binds with high affinity to Ca(2+)/calmodulin and is a substrate for protein kinases A and C. Alternative splicing ... Matsuoka Y, Li X, Bennett V (1998). "Adducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS- ...
Coexpression of SM alpha-actin and desmin was observed in the pericytes of entire capillary segments, and SM alpha-actin was ... Immunohistochemical distribution of vimentin, desmin, glial fibrillary acidic protein and neurofilament proteins in feline ... often forming caps around the nuclear envelope. As the decidual cells grow, the filaments form bundles and nets that radiate ... Alpha-smooth-muscle actin and desmin were demonstrated in the S-type cloned cells by indirect immunofluorescence, as well as by ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... F-actin-capping protein subunit alpha (IPR002189). Short name: CapZ_alpha Overlapping homologous superfamilies *F-actin-capping ... Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Proteins matched: F_ACTIN_CAPPING_A_2 (PS00749) This signature appears in the following proteins: Showing 1 to 20 of 1153 ... Protein name. Species. Domain architecture. A0M8R8 F-actin-capping protein subunit alpha-2. Papio anubis (Olive baboon). ...
Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed ... the F-actin capping protein is a protein which binds in a calcium-independent manner to the fast-growing ends of actin ... Neither of the subunits shows sequence similarity to other filament-capping proteins. The alpha subunit is a protein of about ... "Beta-actinin is equivalent to Cap Z protein". J. Biol. Chem. 265 (15): 8712-5. PMID 2341404. Cooper JA, Caldwell JE, Gattermeir ...
Capping protein controls the addition of actin subunits to the barbed end of actin filaments and nucleates actin polymerization ... capping protein (CapZ) probably binds the barbed ends of actin filaments at the Z line. The in vivo role of this protein in non ... Disruption of the actin cytoskeleton in yeast capping protein mutants.. Amatruda JF1, Cannon JF, Tatchell K, Hug C, Cooper JA. ... indicating that capping protein regulates actin-filament distribution in vivo. ...
Actin Capping Protein. Some articles on actin, actin capping protein, protein:. Capping Protein (actin Filament) Muscle Z-line ... actin capping protein complex ... CAPZB is a member of the F-actin capping protein family ... This gene encodes the beta ... actin capping protein alpha subunit family ... This gene encodes the alpha subunit of the barbed-end actin binding protein ... ... Famous quotes containing the word protein:. "Firm-style bean curd insoles cushion feet, absorb perspiration and provide more ...
F-actin-capping protein subunit alpha-1 is a protein that in humans is encoded by the CAPZA1 gene. CAPZA1 is a member of the F- ... actin capping protein alpha subunit family. This gene encodes the alpha subunit of the barbed-end actin binding protein. The ... 2003). "Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85". J. Biol. Chem. 278 (25): ... "Entrez Gene: CAPZA1 capping protein (actin filament) muscle Z-line, alpha 1". Dawson SJ, White LA (1992). "Treatment of ...
Overexpressing capping protein α and β decreases both F-actin levels and tissue growth, while expressing forms of Capping ... is a master F-actin regulator. In addition to its role in many cellular processes, Capping Protein acts as a main tumor ... We show that the levels and capping activities of both subunits must be tightly regulated to control F-actin levels and ... Protein that have dominant negative effects on F-actin promote tissue growth. Both subunits regulate each others protein ...
... actin filament), gelsolin-like ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews ... capping protein (actin filament), gelsolin-like ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established ... Your search returned 5 capping protein (actin filament), gelsolin-like ELISA ELISA Kit across 2 suppliers. ...
The 100 kDa actin-binding protein from Dictyostelium amoebae is an F-actin capping protein that displays neither severing nor ... This renders capping of actin filaments as the evolutionarily oldest function of an F-actin binding protein. ... The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype (protovillin).. Hofmann A1, Noegel AA, ... which is able to cap actin filaments but still lacks the other villin-type actin-binding activities. ...
Here, we report that actin capping protein (CP), a regulator of actin filament growth, plays an essential role for spine ... Actin Capping Protein Is Required for Dendritic Spine Development and Synapse Formation. Yanjie Fan, Xin Tang, Eric Vitriol, ... 2008) Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell ... 2008) New insights into mechanism and regulation of actin capping protein. Int Rev Cell Mol Biol 267:183-206. ...
Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. The isoform beta-3 ... independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ... F-actin-capping proteins bind in a Ca(2+)- ... View protein in Pfam. PF01115. F_actin_cap_B. 1 hit. Protein ... composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta (CAPZB), ...
Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. ... independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ... F-actin-capping proteins bind in a Ca(2+)- ... View protein in Pfam. PF01115 F_actin_cap_B, 1 hit. Protein ... Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.UniRule annotation. , ...
Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. ... independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ... F-actin-capping proteins bind in a Ca(2+)- ... Capping actin protein of muscle Z-l.... Capping actin protein ... Protein. Similar proteins. Species. Score. Length. Source. Q6NWK1. Capping actin protein of muscle Z-line subunit alpha 1a ( ...
... actin filament), gelsolin-like), Authors: Peeyush Kumar Singh, Ranjan Tamuli. Published in: Atlas Genet Cytogenet Oncol ... protein binding nucleus nucleoplasm nucleolus cytoplasm centriole F-actin capping protein complex protein domain specific ... protein binding nucleus nucleoplasm nucleolus cytoplasm centriole F-actin capping protein complex protein domain specific ... melanosome protein-containing complex binding cadherin binding actin filament binding barbed-end actin filament capping protein ...
Compare capping actin protein of muscle Z-line subunit alpha 2 ELISA Kits from leading suppliers on Biocompare. View ... capping actin protein of muscle Z-line subunit alpha 2 ELISA Kits. Clear ... Your search returned 16 capping actin protein of muscle Z-line subunit alpha 2 ELISA ELISA Kit across 2 suppliers. ... capping actin protein of muscle Z-line subunit alpha 2 ELISA Kits. ...
The actin capping protein (CP) tightly binds to the barbed end of actin filaments, thus playing a key role in actin-based ... The actin capping protein (CP) tightly binds to the barbed end of actin filaments, thus playing a key role in actin-based ... F-actin-capping protein subunit beta isoforms 1 and 2. B. 244. Gallus gallus. Mutation(s): 0 Gene Names: CAPZB. ... F-actin-capping protein subunit alpha-1. A. 286. Gallus gallus. Mutation(s): 0 Gene Names: CAPZA1. ...
... capping actin protein of muscle Z-line subunit beta), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol. ... cytoskeleton organization blood coagulation F-actin capping protein complex regulation of lamellipodium assembly actin ... cytoskeleton organization blood coagulation F-actin capping protein complex regulation of lamellipodium assembly actin ... sarcomere actin cytoskeleton organization cadherin binding actin filament binding barbed-end actin filament capping negative ...
Capping actin protein, gelsolin-like (CapG) was first identified as an actin binding protein of the gelsolin superfamily, which ... CapG, an actin binding protein, modulates the dynamics of the actin cytoskeleton and aberrant turnover of the actin ... The F-actin filament capping protein CapG is a bona fide nucleolar protein. Biochem Biophys Res Commun. 377:699-704. 2008. View ... Actin-capping protein CapG is associated with prognosis, proliferation and metastasis in human glioma. *Authors: *Da-Peng Yun ...
In this study, we investigated the structural aspects of inhibition of actin-capping protein (CP) by phosphatidic acid (PA) and ... These responses are thought to be mediated by dozens of actin-binding proteins, the biochemical activities of which have been ... Our new data shed light on the nature of interactions between peripheral membrane proteins and PA-containing lipid bilayers. In ... our work also significantly contributes to the ongoing debate on structural details of protein interactions with phospholipids. ...
2004) Capping protein binding to actin in yeast: biochemical mechanism and physiological relevance. J Cell Biol 164: 567-580. ... 2012) Capping protein modulates the dynamic behavior of actin filaments in response to phosphatidic acid in Arabidopsis. Plant ... Capping Protein Modulates Actin Remodeling in Response to Reactive Oxygen Species during Plant Innate Immunity. Jiejie Li, ... 2008) New insights into mechanism and regulation of actin capping protein. Int Rev Cell Mol Biol 267: 183-206. ...
... family proteins promote actin polymerization, while Cofilin, Cyclase-associated protein (CAP) and capping proteins (CPs) ... We have found that Capping protein α (Cpa) and Capping protein β (Cpb), which prevent extension of the barbed ends of actin ... Capping protein, Cofilin and CAP all restrict actin filament polymerization (Bamburg, 1999; Gottwald et al., 1996; Schafer et ... Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. J. Biol. Chem. 278,22396 -22403. ...
Capping Protein and Hippo signaling activities inhibit F-actin. ERM proteins can form a structural linkage between ... Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila ... Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila ... Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila ...
Among these molecules, Eps8 is a unique actin binding and signaling protein that possesses actin filament bundling and capping ... regulators of actin dynamics, including actin bundlers and capping proteins, are expected to play a critical role by ... Capping protein increases the rate of actin-based motility by promoting filament nucleation by the Arp2/3 complex. Cell. 2008; ... Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J. Cell Biol. 1997; ...
... "capping protein (actin filament) muscle Z-line, alpha 2")*CCDS: 19926, 19926.1*OMIM: CAPPING PROTEIN, ALPHA-2; CAPZA2*Gene ... capping protein (actin filament) muscle Z-line, alpha 2. Synonyms: 1110053K06Rik, Cappa2. Gene nomenclature, locus information ...
  • A recent study showed that CP is present in dendritic spines of cultured hippocampal neurons and the branched actin filament network containing CP appears to be a prominent feature of the spine head ( Korobova and Svitkina, 2010 ). (jneurosci.org)
  • The aim of the current study is to investigate the relationship between prohibitin ( PHB ), capping actin protein of muscle Z-line beta subunit ( CAPZB ), and tektin-2 ( TEKT2 ) and sperm motility in Murrah buffalo. (ajas.info)
  • We collected the high-motility and low-motility semen samples, testis, ovary, muscle, kidney, liver, brain and pituitary from Murrah buffalo, and analysed the expression of PHB , CAPZB , and TEKT2 in mRNA (message RNA) and protein level. (ajas.info)
  • In vitro analyses of chicken and budding yeast CP revealed that deletions or point mutations in either the α or β tentacles do not affect protein stability but reduce the capping affinity, while a complete removal of both tentacles fully abrogates the actin-binding activity , . (plos.org)
  • For the first time, we report mitogen-activated protein kinase (MAPK) kinase 3 (MKK3) to be up-regulated with glioma invasion in vitro and in vivo . (aacrjournals.org)
  • It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. (proteopedia.org)
  • Similar to findings in fibroblasts in vitro, we show that Ena localises to sites of dynamic actin reorganisation in haemocytes in vivo. (biologists.org)
  • Both fh1 and arpc5 mutations increased actin network density and increased cell shape complexity in pavement cells and trichomes of first true leaves, in contrast to cotyledons. (frontiersin.org)
  • Voltage sensors are integral membrane protein domains that regulate ion channels and enzymes by transporting electrically charged residues across a narrow constriction that focuses the membrane electrical field. (pnas.org)
  • Vinculin - an ABP with cell-cell and cell-matrix junctions, where it is thought to function as one of several interacting proteins involved in anchoring F-actin to the membrane. (tebu-bio.com)
  • The cortical cytoplasm also controls localization of membrane proteins including auxin transporters, contributing thus to cell differentiation and affecting tissue- and organ-scale developmental processes (e.g. (frontiersin.org)
  • Actin assembly drives the extension of flat membrane protrusions called lamellipodia and finger-like protrusions called filopodia to push the membrane. (hindawi.com)
  • Therefore, in the frame of this thesis the structure of the membrane-associated N-terminal domain of D. discoideum CAP was to be determined in cooperation with the group of T. Holak at the MPI f. (uni-muenchen.de)
  • Actin contributes to biological processes such as sensing environmental forces, internalizing membrane vesicles, moving over surfaces, and dividing the cell in two. (sciencemag.org)
  • These two types of actin organization have distinct roles in the cell: the dendritic network in a lamellipodium produces a force that is sufficient to drive membrane protrusion and cell crawling on a planar substrate, whereas the tight actin bundle in a filopodium produces the required stiffness to form a rodlike projection that is believed to be used by the cell to explore the environment and infiltrate between small gaps. (rupress.org)
  • The Z ring is composed of polymers of FtsZ which are attached to the membrane through membrane-associated proteins FtsA and ZipA ( 55 , 56 ). (asm.org)
  • In contrast, WAVE proteins are intrinsically active, but are inhibited in cells by constitutive incorporation into a heteropentameric assembly called the WAVE regulatory complex (WRC, containing WAVE, SRA1, NAP1, ABI, and HSPC300). (pnas.org)
  • Like other aspects of actin assembly, CP is subject to regulation. (pnas.org)
  • Unoccupied WH 2 domains transiently associate with free filament ends, preventing their growth and dynamically tethering the branched actin network to the WASP ‐family proteins that create it. (embopress.org)
  • In the present study, we show that three mutations associated with FSGS, E184K, S186P and R218Q, reduce INF2 auto-inhibition and increase association with monomeric actin. (bris.ac.uk)
  • Furthermore, NVP-BEZ235 fully inhibits the rapamycin-resistant phosphorylation of 4E-BP1, resulting in a marked inhibition of protein translation in AML cells. (aacrjournals.org)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • 7. The expression vector according to claim 5, wherein the recombinant nucleic acid according to claim 1 further comprises a protein coding sequence that encodes a reporter protein or a therapeutic protein. (freepatentsonline.com)
  • 8. An isolated host cell comprising the expression vector of claim 5 wherein the expression vector of claim 5 comprises a protein coding sequence, and the host cell transiently or encoded in the expression vector of claim 5. (freepatentsonline.com)
  • 9. An isolated host cell which is obtained by in vivo injection of the expression vector of claim 5 into a cell, wherein the expression vector of claim 5 comprises a protein coding sequence, and the host cell comprises the expression vector of claim 5 and transiently or encoded in the expression vector of claim 5. (freepatentsonline.com)
  • The alignment of its C-terminal amino acid sequence with the structure of muscle actin predicts a globular, actin-related structure containing all residues that are important for ATP/ADP binding. (uni-muenchen.de)
  • Sequence alignment analyses suggest that the C -terminal region of phostensin, spanning residues 129 to 155, contains a consensus actin-binding motif. (mdpi.com)
  • The 100 kDa actin-binding protein from Dictyostelium amoebae is an F-actin capping protein that displays neither severing nor crosslinking nor nucleating activities [Hofmann et al. (nih.gov)
  • The recently discovered WASH protein (Wiskott-Aldrich syndrome protein and SCAR homologue) is conserved from simple eukaryotes such as Entamoeba and Dictyostelium to humans ( 7 ). (pnas.org)
  • Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum. (mpg.de)
  • The cyclase-associated protein (CAP) from Dictyostelium discoideum was studied in detail regarding its structure and function relationships. (uni-muenchen.de)
  • In dieser Arbeit standen zwei Aufgaben im Mittelpunkt: Zum einen wurde das Cyclase-assoziierte Protein (CAP) aus Dictyostelium discoideum hinsichtlich seiner Struktur-Funktionsbeziehungen eingehend untersucht, zum zweiten erfolgte eine erste Charakterisierung des neuartigen actinähnlichen Proteins Filactin aus D. discoideum. (uni-muenchen.de)
  • To anchor the protrusion, the cell front interacts with the extracellular matrix (ECM) by forming nascent adhesions (or focal complexes) that are connected to the intracellular lamellipodial actin network. (hindawi.com)
  • CP interacts with both actin protomers at the barbed end of the filament, and the amphipathic helix at the C-terminus of the β-subunit binds to the hydrophobic cleft on actin, in a manner similar to that of WH2 domains. (genes2cognition.org)
  • In Drosophila , mutations in either cpa or cpb , lead to accumulation of F-actin within the cell and give rise to identical developmental phenotypes that are tissue specific. (biologists.org)
  • Mutations in inverted formin 2 (INF2), a member of the formin family of actin-regulating proteins, have recently been associated with a familial cause of nephrotic syndrome characterized by FSGS. (bris.ac.uk)
  • From a clinical point of view, we know that mutations in tropomodulin can trigger an accumulation of irregular actin filament bundles, which contribute to nemaline myopathy or other skeletal muscle disorders typified by delayed motor development and muscle weakness. (eurekalert.org)
  • The detailed picture emerging from this study will help shed light on how mutations in tropomodulin, actin, and tropomysin can cause heart disorders. (eurekalert.org)
  • The use of such hybrid regions allows for an efficient protein expression when used in conjunction with circular or linear expression DNA molecules. (freepatentsonline.com)
  • A subset of phagosomes in human macrophages and dendritic cells that is marked by a coat of autophagy-related proteins maintains phagocytosed antigens for prolonged presentation on MHC class II molecules. (rupress.org)
  • This chapter highlights insights gained from recent structural studies as they relate to variations in tropomyosin's coiled-coil structure that are essential for binding to actin and the relationship of periodic repeats to actin molecules in the filament. (springer.com)
  • V-1 completely inhibits CP from interacting with the barbed end, whereas CARMIL proteins act on the barbed end-bound CP and facilitate its dissociation from the filament (called uncapping activity). (rcsb.org)