Cofilin 1: Cofilin 1 is a member of the cofilin family of proteins that is expressed in non-muscle CELLS. It has ACTIN depolymerization activity that is dependent on HYDROGEN-ION CONCENTRATION.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.Destrin: A member of the actin depolymerizing factors. Its depolymerizing activity is independent of HYDROGEN-ION CONCENTRATION.DNA Damage: Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.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.Cofilin 2: A member of the cofilin family of proteins that is expressed in MUSCLE CELLS. It has ACTIN depolymerization activity that is dependent on HYDROGEN-ION CONCENTRATION.Environment: The external elements and conditions which surround, influence, and affect the life and development of an organism or population.Actin Cytoskeleton: Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.DNA Repair: The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.Ataxia Telangiectasia Mutated Proteins: A group of PROTEIN-SERINE-THREONINE KINASES which activate critical signaling cascades in double strand breaks, APOPTOSIS, and GENOTOXIC STRESS such as ionizing ultraviolet A light, thereby acting as a DNA damage sensor. These proteins play a role in a wide range of signaling mechanisms in cell cycle control.Cytoskeleton: The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.Cyanophora: A genus of primitive plants in the family Cyanophoraceae, class GLAUCOPHYTA. They contain pigmented ORGANELLES (or PLASTIDS) called cyanelles, which have characteristics of both CYANOBACTERIA and CHLOROPLASTS.Thiazolidines: Reduced (protonated) form of THIAZOLES. They can be oxidized to THIAZOLIDINEDIONES.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.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Microfilament Proteins: Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.Actin Capping Proteins: Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization.Dendritic Spines: Spiny processes on DENDRITES, each of which receives excitatory input from one nerve ending (NERVE ENDINGS). They are commonly found on PURKINJE CELLS and PYRAMIDAL CELLS.Synapses: Specialized junctions at which a neuron communicates with a target cell. At classical synapses, a neuron's presynaptic terminal releases a chemical transmitter stored in synaptic vesicles which diffuses across a narrow synaptic cleft and activates receptors on the postsynaptic membrane of the target cell. The target may be a dendrite, cell body, or axon of another neuron, or a specialized region of a muscle or secretory cell. Neurons may also communicate via direct electrical coupling with ELECTRICAL SYNAPSES. Several other non-synaptic chemical or electric signal transmitting processes occur via extracellular mediated interactions.Receptors, N-Methyl-D-Aspartate: A class of ionotropic glutamate receptors characterized by affinity for N-methyl-D-aspartate. NMDA receptors have an allosteric binding site for glycine which must be occupied for the channel to open efficiently and a site within the channel itself to which magnesium ions bind in a voltage-dependent manner. The positive voltage dependence of channel conductance and the high permeability of the conducting channel to calcium ions (as well as to monovalent cations) are important in excitotoxicity and neuronal plasticity.Post-Synaptic Density: Cytoskeleton specialization at the cytoplasmic side of postsynaptic membrane in SYNAPSES. It is involved in neuronal signaling and NEURONAL PLASTICITY and comprised of GLUTAMATE RECEPTORS; scaffolding molecules (e.g., PSD95, PSD93), and other proteins (e.g., CaCMKII).Hippocampus: A curved elevation of GRAY MATTER extending the entire length of the floor of the TEMPORAL HORN of the LATERAL VENTRICLE (see also TEMPORAL LOBE). The hippocampus proper, subiculum, and DENTATE GYRUS constitute the hippocampal formation. Sometimes authors include the ENTORHINAL CORTEX in the hippocampal formation.Excitatory Postsynaptic Potentials: Depolarization of membrane potentials at the SYNAPTIC MEMBRANES of target neurons during neurotransmission. Excitatory postsynaptic potentials can singly or in summation reach the trigger threshold for ACTION POTENTIALS.Neurons: The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.Synaptic Transmission: The communication from a NEURON to a target (neuron, muscle, or secretory cell) across a SYNAPSE. In chemical synaptic transmission, the presynaptic neuron releases a NEUROTRANSMITTER that diffuses across the synaptic cleft and binds to specific synaptic receptors, activating them. The activated receptors modulate specific ion channels and/or second-messenger systems in the postsynaptic cell. In electrical synaptic transmission, electrical signals are communicated as an ionic current flow across ELECTRICAL SYNAPSES.Glutamic Acid: A non-essential amino acid naturally occurring in the L-form. Glutamic acid is the most common excitatory neurotransmitter in the CENTRAL NERVOUS SYSTEM.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.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.Blood Proteins: Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.Wheat Germ Agglutinins: Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Plasma: The residual portion of BLOOD that is left after removal of BLOOD CELLS by CENTRIFUGATION without prior BLOOD COAGULATION.Triticum: A plant genus of the family POACEAE that is the source of EDIBLE GRAIN. A hybrid with rye (SECALE CEREALE) is called TRITICALE. The seed is ground into FLOUR and used to make BREAD, and is the source of WHEAT GERM AGGLUTININS.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.Sodium Azide: A cytochrome oxidase inhibitor which is a nitridizing agent and an inhibitor of terminal oxidation. (From Merck Index, 12th ed)Antibodies: Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Azides: Organic or inorganic compounds that contain the -N3 group.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Antibody Formation: The production of ANTIBODIES by proliferating and differentiated B-LYMPHOCYTES under stimulation by ANTIGENS.Ovalbumin: An albumin obtained from the white of eggs. It is a member of the serpin superfamily.Aprotinin: A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)Thermodilution: Measurement of blood flow based on induction at one point of the circulation of a known change in the intravascular heat content of flowing blood and detection of the resultant change in temperature at a point downstream.Epitopes: Sites on an antigen that interact with specific antibodies.Pseudopodia: A dynamic actin-rich extension of the surface of an animal cell used for locomotion or prehension of food.Estradiol: The 17-beta-isomer of estradiol, an aromatized C18 steroid with hydroxyl group at 3-beta- and 17-beta-position. Estradiol-17-beta is the most potent form of mammalian estrogenic steroids.Sexual Behavior, Animal: Sexual activities of animals.Lordosis: The anterior concavity in the curvature of the lumbar and cervical spine as viewed from the side. The term usually refers to abnormally increased curvature (hollow back, saddle back, swayback). It does not include lordosis as normal mating posture in certain animals ( = POSTURE + SEX BEHAVIOR, ANIMAL).Spine: The spinal or vertebral column.Dendrites: Extensions of the nerve cell body. They are short and branched and receive stimuli from other NEURONS.Ventromedial Hypothalamic Nucleus: A nucleus of the middle hypothalamus, the largest cell group of the tuberal region with small-to-medium size cells.Estrous Cycle: The period of cyclic physiological and behavior changes in non-primate female mammals that exhibit ESTRUS. The estrous cycle generally consists of 4 or 5 distinct periods corresponding to the endocrine status (PROESTRUS; ESTRUS; METESTRUS; DIESTRUS; and ANESTRUS).Stem Cell Research: Experimentation on STEM CELLS and on the use of stem cells.Amino Acids, Basic: Amino acids with side chains that are positively charged at physiological pH.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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Fluorescence 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).GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Cell Surface Extensions: Specialized structures of the cell that extend the cell membrane and project out from the cell surface.Liposomes: Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.
(1/626) Structural features of LIM kinase that control effects on the actin cytoskeleton.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

*  SSH1
The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin ... Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T (Feb 2002). "Control of actin reorganization by Slingshot, a family of ... 2006). "Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L". FEBS Lett. 580 (7): 1789-94. doi: ... The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[ ...
*  Actin depolymerizing factor
Actin depolymerizing factors are a family of microfilament proteins. They are used to regulate actin assembly. Actin ... "Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover". J. Biol. Chem. 273 (40 ... Depolymerizing Factors at the US National Library of Medicine Medical Subject Headings (MeSH) Didry D, Carlier MF, Pantaloni D ... "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009-19. doi: ...
*  Pyr1
The latter is the enzyme that uses ATP to phosphorylate and inactivate the actin-depolymerizing factor cofilin. When cofilin is ... LIMK1 also depolymerizes microtubules. In the presence of Pyr1, LIMK1 is inhibited, which means that the phosphorylation of ... Pyr1 may be used in cancer treatment, because its main target enzyme (LIM kinase) is a regulator of microtubule and actin ... In conclusion, Pyr1 inhibits cell motility and controls actin dynamics and stabilizes microtubules. These properties can be ...
*  Destrin
The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of ... This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin ... "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985-93. doi: ... Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene. ...
*  TWF1
2003). "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/ ... Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to ... Palmgren S, Vartiainen M, Lappalainen P (2002). "Twinfilin, a molecular mailman for actin monomers". J. Cell Sci. 115 (Pt 5): ... 2003). "The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers". Mol. Biol. ...
*  Ashish Arora
"NMR assignments of actin depolymerizing factor (ADF) like UNC-60A and cofilin like UNC-60B proteins of Caenorhabditis elegans ...
*  SSH2
The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin ... The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[ ... "Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin". Cell. 108 (2): 233-46 ...
*  Cofilin-2
"The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics". ... Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and ... Bamburg JR, McGough A, Ono S (September 1999). "Putting a new twist on actin: ADF/cofilins modulate actin dynamics". Trends ... 2006). "Cofilin cross-bridges adjacent actin protomers and replaces part of the longitudinal F-actin interface". J. Mol. Biol. ...
*  Axon guidance
While the repulsive cue, Slit, is suggested to stimulate the translation of Cofilin (an actin depolymerizing factor) in growth ... 2006). "Asymmetrical β-actin mRNA translation in growth cones mediates attractive turning to netrin-1". Nature Neuroscience. 9 ... The attractive cue Netrin-1, stimulates mRNA transport and influence synthesis of β-Actin in filopodia of growth cones, to ... and L1 Growth factors like NGF Neurotransmitters and modulators like GABA Growing axons rely on a variety of guidance cues in ...
*  ADF-H domain
"Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin". J ... ADF/cofilins bind ADP-actin with higher affinity than ATP-actin and inhibit the spontaneous nucleotide exchange on actin ... In molecular biology, ADF-H domain (actin-depolymerising factor homology domain) is an approximately 150 amino acid motif that ... They bind both actin-monomers and filaments and promote rapid filament turnover in cells by depolymerising/fragmenting actin ...
*  List of MeSH codes (D05)
Actin depolymerizing factors MeSH D05.750.078.730.212.500 --- cofilin 1 MeSH D05.750.078.730.212.750 --- cofilin 2 MeSH D05.750 ... actin-related protein 2 MeSH D05.750.078.730.246.750 --- actin-related protein 3 MeSH D05.750.078.730.250 --- actins MeSH ... actin capping proteins MeSH D05.750.078.730.032.500 --- capz actin capping protein MeSH D05.750.078.730.032.750 --- ... 212.875 --- destrin MeSH D05.750.078.730.246 --- actin-related protein 2-3 complex MeSH D05.750.078.730.246.500 --- ...
*  Cofilin
... also known as ADF or actin depolymerizing factor Actin-binding proteins regulate assembly and disassembly of actin filaments. ... March 1997). "Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based ... ATP-actin is then available for assembly. Cofilin binds monomeric (G-actin) and filamentous actin (F-actin). Its binding ... "Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in ...
*  Actin remodeling of neurons
Actin Depolymerizing Factor, or ADF, normally disassembles actin and does not allow for the induction of LTP. However, synaptic ... Actin treadmilling is the process of turnover of actin filaments where F-actin is rapidly assembled and disassembled. G-actin ... This protein caps the barbed end of F-actin, thus blocking G-actin subunits to bind to the F-actin and allow for actin ... Actin is only able to cause changes that promote LTP through its formation into F-actin. When F-actin is unable to form, LTD is ...
*  ACTG1
"Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985-93. doi: ... Gamma-actin is eventually replaced by sarcomeric alpha-actin isoforms, with low levels of gamma-actin persisting in adult ... Gamma-actin is a protein that in humans is encoded by the ACTG1 gene. Gamma-actin is widely expressed in cellular cytoskeletons ... Human gamma-actin is 41.8 kDa in molecular weight and 375 amino acids in length. Actins are highly conserved proteins that are ...
*  Tropomyosin
"Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)". Cell Motil. 2 ... it was observed that the actin-binding protein actin depolymerisation factor (ADF)/cofilin, a factor that promotes actin ... The actin filament system that is involved in regulating these cellular pathways is more complex than the actin filament ... The tropomyosin dimer has very low affinity for an actin filament and forms no van der waals contacts with actin. It is only ...
*  ROCK1
... inhibiting its actin-depolymerizing activity. This depolymerization results in stabilization of actin filaments and decreased ... Gilkes DM, Xiang L, Lee SJ, Chaturvedi P, Hubbi ME, Wirtz D, Semenza GL (January 2014). "Hypoxia-inducible factors mediate ... It is a key regulator of actin-myosin contraction, stability, and cell polarity. These contribute to many progresses such as ... This is consistent with its function as a key modulator of cell motility, tumor cell invasion, and actin cytoskeleton ...
*  TUBA1A
Watts NR, Sackett DL, Ward RD, Miller MW, Wingfield PT, Stahl SS, Steven AC (July 2000). "HIV-1 rev depolymerizes microtubules ... Sapir T, Elbaum M, Reiner O (December 1997). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor ... interaction with actin, clathrin and tubulin". The Biochemical Journal. 363 (Pt 3): 599-608. doi:10.1042/0264-6021:3630599. PMC ... Sapir T, Elbaum M, Reiner O (December 1997). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor ...
*  NADPH oxidase
... depolymerized the actin, broke the adhesions, and allowed foam cells to migrate out of the intima. Mutations in the NADPH ... a protein that deactivates certain proangiogenic factors that play a role in the development of the placenta, by facilitating ... These ROSs activate an enzyme that makes the macrophages adhere to the artery wall (by polymerizing actin fibers). This process ...
*  Microtubule
Signals sent between the follicular cells and the oocyte (such as factors similar to epidermal growth factor) cause the ... Recently an actin-like protein has been found in a gram-positive bacterium Bacillus thuringiensis, which forms a microtubule- ... However, once the microtubule depolymerizes, most of these modifications are rapidly reversed by soluble enzymes. Since most ... After nucleation, the minus-ends are released and then re-anchored in the periphery by factors such as ninein and PLEKHA7. In ...
*  CDC42
Miki H, Sasaki T, Takai Y, Takenawa T (January 1998). "Induction of filopodium formation by a WASP-related actin-depolymerizing ... This process is regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, ... "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin- ... Rho GTPases are central to dynamic actin cytoskeletal assembly and rearrangement that are the basis of cell-cell adhesion and ...
*  Rho family of GTPases
Cofilin's function is to reorganize the actin cytoskeleton of a cell; namely, it depolymerizes actin segments and thus inhibits ... NHE1-mediated H+ efflux is required for guanine nucleotide exchange factor (GEF)-catalyzed GTP binding to Cdc42, suggesting a ... G-actin) or filamentous (F-actin) forms. The role of Rho family of GTPases and its effects in the stability of actin and spine ... Cdc42 was assumed to encourage filopodia elongation and block actin depolymerization. RhoA was considered to encourage actin ...
*  Golgi apparatus
Organization of the plant Golgi depends on actin cables and not microtubules. The common feature among Golgi is that they are ... BFA inhibits the function of several guanine nucleotide exchange factors (GEFs) that mediate GTP-binding of ARFs. Treatment of ... If microtubules are experimentally depolymerized, then the Golgi apparatus loses connections and becomes individual stacks ... BFA blocks the activation of some ADP-ribosylation factors (ARFs). ARFs are small GTPases which regulate vesicular trafficking ...
*  LIMK2
... inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the ... "LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-beta ... Sumi T, Matsumoto K, Takai Y, Nakamura T (27 Dec 1999). "Cofilin phosphorylation and actin cytoskeletal dynamics regulated by ... Toshima J, Toshima JY, Takeuchi K, Mori R, Mizuno K (Aug 2001). "Cofilin phosphorylation and actin reorganization activities of ...
*  Cell migration
If so, the actin filaments that form at the front might stabilize the added membrane so that a structured extension, or lamella ... On the other hand high drug concentrations, or microtubule mutations that depolymerize the microtubules, can restore cell ... "2D protrusion but not motility predicts growth factor-induced cancer cell migration in 3D collagen". J. Cell Biol. 197 (6): 721 ... Drugs that destroy actin filaments have multiple and complex effects, reflecting the wide role that these filaments play in ...
Destrin Antibody
		        
	  Destrin Antibody
Protein Aliases: 2610043P17Rik; Actin-depolymerizing factor; ADF; AU042046; bA462D18.2 (destrin (actin depolymerizing factor ... actin polymerization or depolymerization actin filament depolymerization positive regulation of actin filament depolymerization ... actin depolymerizing factor); Dsn; epididymis luminal protein 32; RP23-77A2.1; sID; Sid 23 ...
more infohttps://www.thermofisher.com/antibody/product/Destrin-Antibody-Polyclonal/PA1-24937
SSH1 - Wikipedia  SSH1 - Wikipedia
The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin ... Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T (Feb 2002). "Control of actin reorganization by Slingshot, a family of ... 2006). "Identification of multiple actin-binding sites in cofilin-phosphatase Slingshot-1L". FEBS Lett. 580 (7): 1789-94. doi: ... The SSH family appears to play a role in actin dynamics by reactivating ADF/cofilin proteins in vivo (Niwa et al., 2002).[ ...
more infohttps://en.wikipedia.org/wiki/SSH1
Publications - Actin dynamics  Publications - Actin dynamics
Actin-depolymerizing factor (ADF)/cofilins contribute to cytoskeletal dynamics by promoting rapid actin filament disassembly. ... The contractile actin cortex is a thin layer of actin, myosin, and actin-binding proteins that subtends the membrane of animal ... irrespective of whether the filament is assembled from actin or profilin-actin. Pi release from the depolymerizing barbed end ... Intermittent depolymerization of actin filaments is caused by photo-induced dimerization of actin protomers. ...
more infohttp://www.actindynamics.net/publications
Actin depolymerizing factor - Wikipedia  Actin depolymerizing factor - Wikipedia
Actin depolymerizing factors are a family of microfilament proteins. They are used to regulate actin assembly. Actin ... "Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover". J. Biol. Chem. 273 (40 ... Depolymerizing Factors at the US National Library of Medicine Medical Subject Headings (MeSH) Didry D, Carlier MF, Pantaloni D ... "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009-19. doi: ...
more infohttps://en.wikipedia.org/wiki/Actin_depolymerizing_factor
Plant actin depolymerizing factor: actin microfilament disassembly and more | Springer for Research & Development  Plant actin depolymerizing factor: actin microfilament disassembly and more | Springer for Research & Development
The main function of ADF is the severing and depolymerizing filamentous actin (F-actin), thus regulating F-actin... ... ACTIN DEPOLYMERIZING FACTOR (ADF) is a conserved protein among eukaryotes. ... Actin interacting protein1 and actin depolymerizing factor drive rapid actin dynamics in Physcomitrella patens. Plant Cell 23: ... Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin ...
more infohttps://rd.springer.com/article/10.1007/s10265-016-0899-8
unc-60 - Actin-depolymerizing factor 1, isoforms a/b - Caenorhabditis elegans - unc-60 gene & protein  unc-60 - Actin-depolymerizing factor 1, isoforms a/b - Caenorhabditis elegans - unc-60 gene & protein
Competes with unc-87 for actin binding and inhibits the actin-bundling activity of unc-87 (PubMed:17684058). ... required for the assembly of actin filaments into the functional contractile myofilament lattice of muscle (PubMed:8107682). ... sp,Q07750,ADF1_CAEEL Actin-depolymerizing factor 1, isoforms a/b OS=Caenorhabditis elegans OX=6239 GN=unc-60 PE=1 SV=2 ... Depolymerizes growing actin filaments in muscle cells; required for the assembly of actin filaments into the functional ...
more infohttps://www.uniprot.org/uniprot/Q07750
Overexpression of actin-depolymerizing factor blocks oxidized low-density lipoprotein-induced mouse brain microvascular...  Overexpression of actin-depolymerizing factor blocks oxidized low-density lipoprotein-induced mouse brain microvascular...
... an important regulator of actin cytoskeleton, in the oxidized low-density lipoprotein (ox-LDL)-induced... ... The aim of present work was to elucidate the role of actin-depolymerizing factor (ADF), ... Actin-depolymerizing factor Endothelial Blood-brain barrier Reactive oxygen species Actin cytoskeleton ... The aim of present work was to elucidate the role of actin-depolymerizing factor (ADF), an important regulator of actin ...
more infohttps://link.springer.com/article/10.1007%2Fs11010-012-1415-7
IJMS | Free Full-Text | The Actin Depolymerizing Factor (ADF)/Cofilin Signaling Pathway and DNA Damage Responses in Cancer  IJMS | Free Full-Text | The Actin Depolymerizing Factor (ADF)/Cofilin Signaling Pathway and DNA Damage Responses in Cancer
Cofilin-1 (CFL-1) is a primary non-muscle isoform of the ADF/cofilin protein family accelerating the actin filamental turnover ... In response to environmental stimulation, CFL-1 enters the nucleus to regulate the actin dynamics. Although the purpose of this ... cofilin protein family is essential for actin dynamics, cell division, chemotaxis and tumor metastasis. ... The actin depolymerizing factor (ADF)/cofilin protein family is essential for actin dynamics, cell division, chemotaxis and ...
more infohttp://www.mdpi.com/1422-0067/16/2/4095
Actin-depolymerizing factor elisa and antibody  Actin-depolymerizing factor elisa and antibody
Recombinant Protein and Actin-depolymerizing factor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody ... Actin-depolymerizing factor 1. Actin-depolymerizing factor 1 ELISA Kit. Actin-depolymerizing factor 1 Recombinant. Actin- ... Actin-depolymerizing factor 10. Actin-depolymerizing factor 10 ELISA Kit. Actin-depolymerizing factor 10 Recombinant. Actin- ... Actin-depolymerizing factor 11. Actin-depolymerizing factor 11 ELISA Kit. Actin-depolymerizing factor 11 Recombinant. Actin- ...
more infohttps://www.mybiosource.com/protein_family.php?root=actin-depolymerizing-factor
Actin Depolymerizing Factors Cofilin1 and Destrin Are Required for Ureteric Bud Branching Morphogenesis | proLékaře.cz  Actin Depolymerizing Factors Cofilin1 and Destrin Are Required for Ureteric Bud Branching Morphogenesis | proLékaře.cz
2002 The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics ... Actin Depolymerizing Factors Cofilin1 and Destrin Are Required for Ureteric Bud Branching Morphogenesis Download PDF České info ... proLékaře.cz / Odborné časopisy / PLOS Genetics / 2010 - 10 / Actin Depolymerizing Factors Cofilin1 and Destrin Are Required ... 2005 The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev ...
more infohttps://www.prolekare.cz/casopisy/plos-genetics/2010-10/actin-depolymerizing-factors-cofilin1-and-destrin-are-required-for-ureteric-bud-branching-morphogenesis-45088
ADF (Actin Depolymerizing Factor): The Breaker of the Polymer in Homeostasis | Springer for Research & Development  ADF (Actin Depolymerizing Factor): The Breaker of the Polymer in Homeostasis | Springer for Research & Development
Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol ... Hawkins M, Pope B, Maciver SK, Weeds AG (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin ... Mehta S, Sibley LD (2010) Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J Biol Chem 285(9 ... Funk JD, Bamburg JR (2007) Proteins of the actin depolymerizing factor/Cofilin family. In: Actin-monomer-binding proteins. ...
more infohttps://rd.springer.com/chapter/10.1007%2F978-981-13-7450-0_5
Plantae | Loose-Knit Family: Tracing the Evolution of Actin Depolymerizing Factors that Sever or Join the Actin Cytoskeleton |...  Plantae | Loose-Knit Family: Tracing the Evolution of Actin Depolymerizing Factors that Sever or Join the Actin Cytoskeleton |...
... aspb.org The interior of a plant cell is supported by the actin cytoskeleton, a complex network of yarn-like fibers… ... such as actin depolymerizing factors (ADFs). ADFs can bind to both monomeric and filamentous actin (F-actin). Across the plant ... Loose-Knit Family: Tracing the Evolution of Actin Depolymerizing Factors that Sever or Join the Actin Cytoskeleton January 31, ... depolymerizing F-actin) ADFs, which sever or depolymerize F-actin and 2) B-type (bundling F-actin) ADFs, which bind to and ...
more infohttps://plantae.org/loose-knit-family-tracing-the-evolution-of-actin-depolymerizing-factors-that-sever-or-join-the-actin-cytoskeleton/
Comprehensive analysis of differentially expressed rice actin depolymerizing factor gene family and heterologous overexpression...  Comprehensive analysis of differentially expressed rice actin depolymerizing factor gene family and heterologous overexpression...
... are small actin-binding proteins. Many higher-plant ADFs has been known to involve in plant growth, development and pathogen ... Actin depolymerizing factors (ADFs) are small actin-binding proteins. Many higher-plant ADFs has been known to involve in plant ... Staiger CJ, Gibbon BC, Kovar DR, Zonia LE: Profilin and actin-depolymerizing factor: modulators of actin organization in plants ... Actin-depolymerizing factor 2-mediated actin dynamics are essential for root-knot nematode infection of Arabidopsis. Plant Cell ...
more infohttps://thericejournal.springeropen.com/articles/10.1186/1939-8433-5-33
A Mechanism for Actin Filament Severing by Malaria Parasite Actin Depolymerizing Factor 1 via a Low Affinity Binding Interface ...  A Mechanism for Actin Filament Severing by Malaria Parasite Actin Depolymerizing Factor 1 via a Low Affinity Binding Interface ...
A Mechanism for Actin Filament Severing by Malaria Parasite Actin Depolymerizing Factor 1 via a Low Affinity Binding Interface ...
more infohttps://findanexpert.unimelb.edu.au/display/publication252655
Shank3 Deficiency Induces NMDA Receptor Hypofunction via an Actin-Dependent Mechanism | Journal of Neuroscience  Shank3 Deficiency Induces NMDA Receptor Hypofunction via an Actin-Dependent Mechanism | Journal of Neuroscience
1993) Isolation and characterization of a regulated form of actin depolymerizing factor. J Cell Biol 122:623-633, doi:10.1083/ ... Cofilin, the major actin depolymerizing factor, is required for Shank3 regulation of NMDAR currents.. Next, we examined the ... 1995) Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270: ... Inhibiting cofilin, the primary downstream target of PAK and a major actin depolymerizing factor, prevented Shank3 siRNA from ...
more infohttp://www.jneurosci.org/content/33/40/15767
Recombinant Human Gelsolin plasma protein (ab114279)  Recombinant Human Gelsolin plasma protein (ab114279)
Actin depolymerizing factor. *ADF. *AGEL. *Brevin. *Gelsolin. see all. * Relevance. Gelsolin is a calcium regulated, actin ... and severs actin filaments in the presence of submicromolar calcium, thereby solating cytoplasmic actin gels. A calcium ... It plays a role in phosphoinositide mediated disassembly of actin filaments in Sertoli cell adhesion complexes; it may regulate ... modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end ...
more infohttp://www.abcam.com/recombinant-human-gelsolin-plasma-protein-ab114279.html
Recombinant Human Gelsolin/GSN Protein (H00002934-P01): Novus Biologicals  Recombinant Human Gelsolin/GSN Protein (H00002934-P01): Novus Biologicals
Actin-depolymerizing factor. *ADF. *AGEL. *Brevin. *DKFZp313L0718. *gelsolin (amyloidosis, Finnish type). *Gelsolin ... The protein encoded by this gene binds to the "plus" ends of actin monomers and filaments to prevent monomer exchange. The ... encoded calcium-regulated protein functions in both assembly and disassembly of actin filaments. Defects in this gene are a ...
more infohttps://www.novusbio.com/products/gelsolin-gsn-recombinant-protein_h00002934-p01
ml, 1 mg, 200 µl Ovalbumin Antibody (Monoclonal from Thermo Fisher Scientific, Inc.  ml, 1 mg, 200 µl Ovalbumin Antibody (Monoclonal from Thermo Fisher Scientific, Inc.
Brevin; Actin-depolymerizing factor; AGEL *View Details. *Images. *Ref. Catalog #. Size. Price (AUD). Your Price (AUD) Qty. ... Williams-Fitzgerald-Flaujeac factor; High molecular weight kininogen; Fitzgerald factor; Alpha-2-thiol proteinase inhibitor ...
more infohttp://www.thermofisher.com/1/1/indexc31.html
Complement receptor-3 negatively regulates the phagocytosis of degenerated myelin through tyrosine kinase Syk and cofilin |...  Complement receptor-3 negatively regulates the phagocytosis of degenerated myelin through tyrosine kinase Syk and cofilin |...
Active cofilin could advance phagocytosis by promoting F-actin remodeling, which supports the production of membrane ... filamentous actin) remodeling (i.e., disassembly and reassembly) by shifting between active unphosphorylated and inactive ... Cofilin is an actin-depolymerizing protein that controls F-actin ( ... Cofilin/ADF (actin depolymerizing factor) is a family of proteins that controls F-actin remodeling and thereby the production ...
more infohttps://jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-166
Recombinant Human GSN 293 Cell Lysate GSN-5722HCL - Creative BioMart  Recombinant Human GSN 293 Cell Lysate GSN-5722HCL - Creative BioMart
... actin-depolymerizing factor; ADF; AGEL;. ... Actin etc Proteins > Actin Assembly Proteins Actin Assembly ...
more infohttps://www.creativebiomart.net/description_407388_318.htm
  • 1995 ). It was also shown that Arabidopsis thaliana ADF1 (AtADF1) increases assembly of F-actin at higher concentration (Carlier et al. (springer.com)
  • The actin depolymerizing factors (ADFs) play important roles in several cellular processes that require cytoskeletal rearrangements, such as cell migration, but little is known about the in vivo functions of ADFs in developmental events like branching morphogenesis. (prolekare.cz)
  • Most ADFs exhibited F-actin-severing activity. (plantae.org)
  • The ADFs were divided into two categories based on activity: 1) D-type ( d epolymerizing F-actin) ADFs, which sever or depolymerize F-actin and 2) B-type ( b undling F-actin) ADFs, which bind to and bundle F-actin. (plantae.org)
  • We also show that the molecular dynamic properties of F-BAR(2) at the membrane are partially dependent on F-Actin. (biologists.org)
  • Here, we demonstrate that rapid actin remodeling upon elicitation with diverse microbe-associated molecular patterns and damage-associated molecular patterns represent a conserved plant immune response. (plantphysiol.org)
  • PRRs directly sense conserved microbe-associated molecular patterns (MAMPs), such as bacterial flagellin and elongation factor-Tu, as well as chitin from fungal cell walls. (plantphysiol.org)
  • 1997 ). The interaction between actin and ADF is regulated by reversible phosphorylation, pH, and specific phosphoinositides (Allwood et al. (springeropen.com)
  • Polarized growth of pollen tubes or root hair cells requires molecule delivery to the growing apex through F-actin. (springer.com)
  • Actin, including both globular (G) and filamentous (F), regulates various cellular functions that are necessary for plants to grow and respond to environmental changes. (springer.com)
  • 1993 ). Biochemical characterization of plant ADF was first performed with Zea mays ADF3 (ZmABP3 then renamed as ZmADF3), confirming its conserved activity to bind both F- and G-actin (Rozycka et al. (springer.com)
  • Plant actin-depolymerizing factors possess opposing biochemical properties arising from key amino acid changes throughout evolution. (plantae.org)
  • Kanellos G, Zhou J, Patel H et al (2015) ADF and cofilin1 control actin stress fibers, nuclear integrity, and cell survival. (springer.com)
  • Actin fibers readily come apart (sever) and join back together, depending on the needs of the cell. (plantae.org)
  • 2010 ). F-actin also plays important roles in responses against microbial attacks (Day et al. (springer.com)
  • Actin remodeling requires ROS generated by the defense-associated NADPH oxidase, RBOHD. (plantphysiol.org)
  • Moreover, perception of flg22 by its cognate receptor complex triggers actin remodeling through the activation of RBOHD-dependent ROS production. (plantphysiol.org)
  • Additionally, we uncover a negative feedback loop between actin remodeling and flg22-induced ROS production. (plantphysiol.org)
  • The pathways for actin remodeling during innate immune signaling are both parallel and convergent, and potentially tissue-specific. (plantphysiol.org)
  • These critical clock neurons express the neuropeptide pigment dispersing factor (PDF) ( Helfrich-Forster, 1995 , 2005 ), which has long been proposed to serve as the clock output mediating coordination of downstream neurons. (frontiersin.org)