Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin.
Authors Dan C; Kelly A; Bernard O; Minden A;
JournalJ Biol Chem
PubMed ID11413130
'PAK4 is the most recently identified member of the PAK family of serine/threonine kinases. PAK4 differs from other members of the PAK family in sequence and in many of its functions. Previously, we have shown that an important function of this kinase is to mediate the induction of filopodia in ... More
'Tropomyosin binds to actin filaments and is implicated in stabilization of actin cytoskeleton. We examined biochemical and cell biological properties of Caenorhabditis elegans tropomyosin (CeTM) and obtained evidence that CeTM is antagonistic to ADF/cofilin-dependent actin filament dynamics. We purified CeTM, actin, and UNC-60B (a muscle-specific ADF/cofilin isoform), all of which ... More
Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion.
AuthorsChan AY, Bailly M, Zebda N, Segall JE, Condeelis JS
JournalJ Cell Biol
PubMed ID10662778
'Stimulation of metastatic MTLn3 cells with epidermal growth factor (EGF) causes a rapid and transient increase in actin nucleation activity resulting from the appearance of free barbed ends at the extreme leading edge of extending lamellipods. To investigate the role of cofilin in EGF-stimulated actin polymerization and lamellipod extension in ... More
The platelet cytoskeleton regulates the affinity of the integrin alpha(IIb)beta(3) for fibrinogen.
AuthorsBennett JS, Zigmond S, Vilaire G, Cunningham ME, Bednar B
JournalJ Biol Chem
PubMed ID10464255
'Agonist-generated inside-out signals enable the platelet integrin alpha(IIb)beta(3) to bind soluble ligands such as fibrinogen. We found that inhibiting actin polymerization in unstimulated platelets with cytochalasin D or latrunculin A mimics the effects of platelet agonists by inducing fibrinogen binding to alpha(IIb)beta(3). By contrast, stabilizing actin filaments with jasplakinolide prevented ... More
Low molecular-weight G-actin binding proteins involved in the regulation of actin assembly during myofibrillogenesis.
AuthorsObinata T, Nagaoka-Yasuda R, Ono S, Kusano K, Mohri K, Ohtaka Y, Yamashiro S, Okada K, Abe H
JournalCell Struct Funct
PubMed ID9113405
'We previously demonstrated that small G-actin binding proteins, cofilin, ADF and profilin, are involved in the actin dynamics during myofibrillogenesis (OBINATA, T. (1993). Int. Rev. Cytol., 143: 153-189.). To better understand how they are responsible for the regulation of actin assembly, the amounts of the actin-binding proteins were quantified by ... More
A protein kinase from neutrophils that specifically recognizes Ser-3 in cofilin.
AuthorsLian JP, Marks PG, Wang JY, Falls DL, Badwey JA
JournalJ Biol Chem
PubMed ID10644754
'Cofilin promotes the depolymerization of actin filaments, which is required for a variety of cellular responses such as the formation of lamellipodia and chemotaxis. Phosphorylation of cofilin on serine residue 3 is known to block these activities. We now report that neutrophils contain a protein kinase that selectively catalyzes the ... More
Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments.
AuthorsBlanchoin L, Pollard TD
JournalJ Biol Chem
PubMed ID10336448
'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 ... More
The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin.
AuthorsMaciver SK, Pope BJ, Whytock S, Weeds AG
JournalEur J Biochem
PubMed ID9760179
'Actin depolymerizing factor (ADF) from vertebrates and actophorin from Acanthamoeba castellanii are members of a protein family that bind monomeric and polymeric actin and have been shown by microscopy to sever filaments. Here, we compare the properties of recombinant human ADF and actophorin using rabbit muscle actin. ADF binds tenfold ... More
Cofilin promotes rapid actin filament turnover in vivo.
AuthorsLappalainen P, Drubin DG
JournalNature
PubMed ID9214506
'The ability of actin filaments to function in cell morphogenesis and motility is coupled to their capacity for rapid assembly and disassembly. Because disassembly in vitro is much slower than in vivo, cellular factors that stimulate disassembly have long been assumed to exist. Although numerous proteins can affect actin dynamics ... More
The C-terminal tail of UNC-60B (actin depolymerizing factor/cofilin) is critical for maintaining its stable association with F-actin and is implicated in the second actin-binding site.
AuthorsOno S, McGough A, Pope BJ, Tolbert VT, Bui A, Pohl J, Benian GM, Gernert KM, Weeds AG
JournalJ Biol Chem
PubMed ID11050090
'Actin depolymerizing factor (ADF)/cofilin changes the twist of actin filaments by binding two longitudinally associated actin subunits. In the absence of an atomic model of the ADF/cofilin-F-actin complex, we have identified residues in ADF/cofilin that are essential for filament binding. Here, we have characterized the C-terminal tail of UNC-60B (a ... More
Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium.
AuthorsAizawa H, Sutoh K, Yahara I
JournalJ Cell Biol
PubMed ID8636212
'Cofilin is a low molecular weight actin-modulating protein whose structure and function are conserved among eucaryotes. Cofilin exhibits in vitro both a monomeric actin-sequestering activity and a filamentous actin-severing activity. To investigate in vivo functions of cofilin, cofilin was overexpressed in Dictyostelium discoideum cells. An increase in the content of ... More
Differential regulation of actin depolymerizing factor and cofilin in response to alterations in the actin monomer pool.
AuthorsMinamide LS, Painter WB, Schevzov G, Gunning P, Bamburg JR
JournalJ Biol Chem
PubMed ID9079652
'Myoblasts, transfected with a human gene encoding a beta-actin point mutation, down-regulate expression of actin depolymerizing factor (ADF) and its mRNA. Regulation is posttranscriptional. Expression of cofilin, a structurally similar protein, and profilin, CapG, and tropomodulin is not altered with increasing mutant beta-actin expression. Myoblasts expressing either human gamma-actin or ... More
Cofilin undergoes rapid dephosphorylation in stimulated neutrophils and translocates to ruffled membranes enriched in products of the NADPH oxidase complex. Evidence for a novel cycle of phosphorylation and dephosphorylation.
AuthorsHeyworth PG, Robinson JM, Ding J, Ellis BA, Badwey JA
JournalHistochem Cell Biol
PubMed ID9342616
'Neutrophils contain a 21-kDa phosphoprotein that undergoes rapid dephosphorylation upon stimulation of these cells with the chemoattractant N-fMet-Leu-Phe (fMLP), activators of protein kinase C [e.g., 4 beta-phorbol 12-myristate 13-acetate (PMA)] or the calcium ionophore A23187. This phosphoprotein was identified as the non-muscle form of cofilin by peptide sequencing and immunoblotting ... More
Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor.
AuthorsAdams ME, Minamide LS, Duester G, Bamburg JR
JournalBiochemistry
PubMed ID2223773
'Chick brain actin depolymerizing factor (ADF) is a 19-kDa protein that severs actin filaments and binds actin monomers. We have obtained a cDNA encoding ADF by screening a chick embryo lambda gt11 cDNA library with both a rabbit anti-ADF antiserum and two oligonucleotide probes. Several non-full-length clones of 636 bases ... More
Control of actin filament length and turnover by actin depolymerizing factor (ADF/cofilin) in the presence of capping proteins and ARP2/3 complex.
'The effect of Arabidopsis thaliana ADF1 and human ADF on the number of filaments in F-actin solutions has been examined using a seeded polymerization assay. ADF did not sever filaments in a catalytic fashion, but decreased the steady-state length distribution of actin filaments in correlation with its effect on actin ... More
Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function.
AuthorsMcGough A, Pope B, Chiu W, Weeds A
JournalJ Cell Biol
PubMed ID9265645
'Cofilin is an actin depolymerizing protein found widely distributed in animals and plants. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on actin filaments. Cofilin binds filamentous (F)-actin cooperatively by bridging two longitudinally associated actin subunits. The binding site is centered axially at subdomain 2 ... More
Herbimycin A inhibits both dephosphorylation and translocation of cofilin induced by opsonized zymosan in macrophagelike U937 cells.
'We previously reported that a 21-kDa phosphoprotein may play an important role in superoxide production through dephosphorylation by neutrophillike differentiated HL-60 cells (Suzuki et al., 1995, Biochim Biophys Acta 1266: 261-267). The phosphoprotein was identified as cofilin, an actin-binding protein, and the activation-induced changes in its intracellular distribution have been ... More
Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation.
AuthorsRessad F, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D, Carlier MF
JournalJ Biol Chem
PubMed ID9694836
'The thermodynamics and kinetics of actin interaction with Arabidopsis thaliana actin-depolymerizing factor (ADF)1, human ADF, and S6D mutant ADF1 protein mimicking phosphorylated (inactive) ADF are examined comparatively. ADFs interact with ADP.G-actin in rapid equilibrium (k+ = 155 microM-1.s-1 and k- = 16 s-1 at 4 degreesC under physiological ionic conditions). ... More
Control of actin assembly and disassembly at filament ends.
AuthorsCooper JA, Schafer DA
JournalCurr Opin Cell Biol
PubMed ID10679358
'The most important discovery in the field is that the Arp2/3 complex nucleates assembly of actin filaments with free barbed ends. Arp2/3 also binds the sides of actin filaments to create a branched network. Arp2/3''s nucleation activity is stimulated by WASP family proteins, some of which mediate signaling from small ... More
Regulation of actin dynamics: The LIM kinase connection.
AuthorsLawler S
JournalCurr Biol
PubMed ID10556082
'A signalling pathway has recently been delineated that connects Rho-family GTPases to the cytoskeleton via LIM kinase and the F-actin depolymerising protein cofilin. The existence of this pathway helps to explain some of the effects of LIM kinase and cofilin in the control of actin dynamics.' ... More
Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis.
AuthorsNagaoka R, Abe H, Kusano K, Obinata T
JournalCell Motil Cytoskeleton
PubMed ID7728864
'Cofilin is a small actin-binding protein which regulates actin polymerization in a pH-dependent manner. Immunofluorescence microscopy with a monoclonal antibody for cofilin revealed that this protein is temporarily concentrated at the contractile ring during cytokinesis. Cofilin appeared to accumulate rapidly at the contractile ring during late stages of furrowing, and ... More
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin.
AuthorsBlanchoin L, Pollard TD
JournalJ Biol Chem
PubMed ID9737968
'Acanthamoeba actophorin is a member of ADF/cofilin family that binds both actin monomers and filaments. We used fluorescence anisotropy to study the interaction of actin monomers with recombinant actophorin labeled with rhodamine on a cysteine substituted for Serine-88. Labeled actophorin retains its affinity for actin and ability to reduce the ... More
Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes.
AuthorsAbe H, Nagaoka R, Obinata T
JournalExp Cell Res
PubMed ID8482351
'We used immunofluorescence methods to examine the cellular distribution of cofilin in chicken myotubes in primary culture. Cofilin showed mainly diffuse distribution in the cytoplasm except for rather strong staining around the nuclei and faint striated patterns along myofibrils, but did not stain inside the nuclei. Neither stress fiber-like structures ... More
Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells.
AuthorsPendleton A, Pope B, Weeds A, Koffer A
JournalJ Biol Chem
PubMed ID12566455
'Increasing cellular G-actin, using latrunculin B, in either intact or permeabilized rat peritoneal mast cells, caused translocation of both actin and an actin regulatory protein, cofilin, into the nuclei. The effect was not associated with an increase in the proportion of apoptotic cells. The major part of the nuclear actin ... More
Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase.
AuthorsArber S, Barbayannis FA, Hanser H, Schneider C, Stanyon CA, Bernard O, Caroni P
JournalNature
PubMed ID9655397
'Cell division, cell motility and the formation and maintenance of specialized structures in differentiated cells depend directly on the regulated dynamics of the actin cytoskeleton. To understand the mechanisms of these basic cellular processes, the signalling pathways that link external signals to the regulation of the actin cytoskeleton need to ... More
Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia.
AuthorsSvitkina TM, Borisy GG
JournalJ Cell Biol
PubMed ID10352018
'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 ... More
The identification of a second cofilin binding site on actin suggests a novel, intercalated arrangement of F-actin binding.
AuthorsRenoult C, Ternent D, Maciver SK, Fattoum A, Astier C, Benyamin Y, Roustan C
JournalJ Biol Chem
PubMed ID10506133
'The cofilins are members of a protein family that binds monomeric and filamentous actin, severs actin filaments, and increases monomer off-rate from the pointed end. Here, we characterize the cofilin-actin interface. We confirm earlier work suggesting the importance of the lower region of subdomain 1 encompassing the N and C ... More
A role of cofilin/destrin in reorganization of actin cytoskeleton in response to stresses and cell stimuli.
AuthorsYahara I, Aizawa H, Moriyama K, Iida K, Yonezawa N, Nishida E, Hatanaka H, Inagaki F
JournalCell Struct Funct
PubMed ID9118250
'1. Cofilin is an essential actin-regulating protein widely distributed in all eucaryotes. The structure and function of cofilin are conserved during evolution. 2. Cofilin depolymerizes F-actin in vitro at alkaline pH and severs F-actin in vitro at pH lower than 7.3. Overexpression of cofilin in viable cells induced bundles of ... More
Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover.
AuthorsDidry D, Carlier MF, Pantaloni D
JournalJ Biol Chem
PubMed ID9748225
'The mechanism of control of the steady state of actin assembly by actin depolymerizing factor (ADF)/cofilin and profilin has been investigated. Using Tbeta4 as an indicator of the concentration of ATP-G-actin, we show that ADF increases the concentration of ATP-G-actin at steady state. The measured higher concentration of ATP-G-actin is ... More
Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility.
AuthorsCarlier MF, Laurent V, Santolini J, Melki R, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D
JournalJ Cell Biol
PubMed ID9087445
'Actin-binding proteins of the actin depolymerizing factor (ADF)/cofilin family are thought to control actin-based motile processes. ADF1 from Arabidopsis thaliana appears to be a good model that is functionally similar to other members of the family. The function of ADF in actin dynamics has been examined using a combination of ... More
Opposite effects of cofilin and profilin from porcine brain on rate of exchange of actin-bound adenosine 5'-triphosphate.
AuthorsNishida E
JournalBiochemistry
PubMed ID4096896
'Cofilin, an actin-binding protein isolated from porcine brain that reacts with actin in a 1:1 molar ratio [Nishida, E., Maekawa, S., & Sakai, H. (1984) Biochemistry 23, 5307-5313], decreases the rate of exchange of ATP bound to G-actin with 1,N6-ethenoadenosine 5''-triphosphate in solution. From analyses of the dependence of the ... More
Control of actin dynamics in cell motility. Role of ADF/cofilin.
AuthorsCarlier MF, Ressad F, Pantaloni D
JournalJ Biol Chem
PubMed ID10567336
Cell motility. Bare bones of the cytoskeleton.
AuthorsMachesky LM, Cooper JA
JournalNature
PubMed ID10524617
Putting a new twist on actin: ADF/cofilins modulate actin dynamics.
AuthorsBamburg JR, McGough A, Ono S
JournalTrends Cell Biol
PubMed ID10461190
The actin-depolymerizing factor (ADF)/cofilins are a family of essential actin regulatory proteins, ubiquitous among eukaryotes, that enhance the turnover of actin by regulating the rate constants of polymerization and depolymerization at filament ends, changing the twist of the filament and severing actin filaments. Genetic and cell-biological studies have shown that ... More
Actin depolymerizing factor is a component of slow axonal transport.
AuthorsBray JJ, Fernyhough P, Bamburg JR, Bray D
JournalJ Neurochem
PubMed ID1374117
We examined the low molecular weight proteins transported with actin in the chicken sciatic nerve after injection of [35S]methionine into the lumbar spinal cord. A prominent component of slow axonal transport with apparent molecular mass 19 kDa comigrated on two-dimensional gels with chicken actin depolymerizing factor (ADF), previously shown to ... More
ADF/cofilin weakens lateral contacts in the actin filament.
AuthorsMcGough A, Chiu W
JournalJ Mol Biol
PubMed ID10448032
Observed in vivo motility rates can only be accounted for if the rate of actin filament treadmilling in cells is considerably greater than has been quantified for purified actin in vitro. ADF/cofilin is uniquely suited to promote actin dynamics in cells, owing to its remarkable ability to change actin filament ... More
Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics.
AuthorsEdwards DC, Sanders LC, Bokoch GM, Gill GN
JournalNat Cell Biol
PubMed ID10559936
Extracellular signals regulate actin dynamics through small GTPases of the Rho/Rac/Cdc42 (p21) family. Here we show that p21-activated kinase (Pak1) phosphorylates LIM-kinase at threonine residue 508 within LIM-kinase's activation loop, and increases LIM-kinase-mediated phosphorylation of the actin-regulatory protein cofilin tenfold in vitro. In vivo, activated Rac or Cdc42 increases association ... More
Colocalization of ADF and cofilin in intranuclear actin rods of cultured muscle cells.
AuthorsOno S, Abe H, Nagaoka R, Obinata T
JournalJ Muscle Res Cell Motil
PubMed ID8315023
Immunofluorescence microscopy revealed that two actin-binding proteins of low molecular weight with different functional activity, ADF and cofilin, are transported into nuclei of cultured myogenic cells to form rod structures there together with actin, when the cells were incubated in medium containing dimethylsulfoxide. In most cases, ADF and cofilin colocalized ... More
An actin-interacting heptapeptide in the cofilin sequence.
AuthorsYonezawa N, Nishida E, Ohba M, Seki M, Kumagai H, Sakai H
JournalEur J Biochem
PubMed ID2753044
Cofilin, a 21-kDa actin-binding protein, has a hexapeptide sequence DAIKKK which is identical to the N-terminal portion (residues 2-7) of tropomyosin. The synthetic heptapeptide, DAIKKKL, corresponding to residues 122-128 of cofilin, inhibited the binding of cofilin to F-actin in a dose-dependent manner. The heptapeptide cosedimented with F-actin, decreased the fluorescence ... More
pH control of actin polymerization by cofilin.
AuthorsYonezawa N, Nishida E, Sakai H
JournalJ Biol Chem
PubMed ID4055781
Cofilin, a 21,000 molecular weight actin-regulatory protein (Nishida, E., Maekawa, S., and Sakai, H. (1984) Biochemistry 23, 5307-5313), was here shown to be capable of reversibly controlling actin polymerization and depolymerization in a pH-sensitive manner. When cofilin was reacted with F-actin at different pH, the depolymerized actin concentration (= monomeric ... More
Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin.
AuthorsYonezawa N, Nishida E, Iida K, Kumagai H, Yahara I, Sakai H
JournalJ Biol Chem
PubMed ID2037594
Cofilin is an F-actin side-binding and -depolymerizing protein with an apparent molecular mass of 21 kDa. By means of the end label fingerprinting method, the amino acid residue on cofilin sequence cross-linked to actin by zero length cross-linker, 1-ethyl-3-(3-dimethylamino propyl)carbodiimide, was identified as Lys112 and/or Lys114. A synthetic dodecapeptide patterned ... More
Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase.
AuthorsMaekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S
JournalScience
PubMed ID10436159
The actin cytoskeleton undergoes extensive remodeling during cell morphogenesis and motility. The small guanosine triphosphatase Rho regulates such remodeling, but the underlying mechanisms of this regulation remain unclear. Cofilin exhibits actin-depolymerizing activity that is inhibited as a result of its phosphorylation by LIM-kinase. Cofilin was phosphorylated in N1E-115 neuroblastoma cells ... More
Proteins of the ADF/cofilin family: essential regulators of actin dynamics.
AuthorsBamburg JR
JournalAnnu Rev Cell Dev Biol
PubMed ID10611961
Ubiquitous among eukaryotes, the ADF/cofilins are essential proteins responsible for the high turnover rates of actin filaments in vivo. In vertebrates, ADF and cofilin are products of different genes. Both bind to F-actin cooperatively and induce a twist in the actin filament that results in the loss of the phalloidin-binding ... More
Axonal transport and distribution of cyclophilin A in chicken neurones.
AuthorsYuan A, Mills RG, Bamburg JR, Bray JJ
JournalBrain Res
PubMed ID9401740
In the course of pulse-label studies on the axonal transport of the small, basic, actin-binding proteins--actin depolymerizing factor, cofilin and profilin--in chicken motor neurones, we observed a heavily labelled protein of M(r) 18 kDa and pI 8.2 on fluorographs of two-dimensional polyacrylamide gels. On the basis of its M(r), pI ... More
Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells.
AuthorsNishida E, Iida K, Yonezawa N, Koyasu S, Yahara I, Sakai H
JournalProc Natl Acad Sci U S A
PubMed ID3474653
Incubation of cultured cells under specific conditions induces a dramatic change in the actin organization: induction of intranuclear and/or cytoplasmic actin rods (actin paracrystal-like intracellular structures). We have found that cofilin, a 21-kDa actin-binding protein, is a component of these rods. Antibodies directed against cofilin labeled intranuclear actin rods induced ... More
Aip1p interacts with cofilin to disassemble actin filaments.
AuthorsRodal AA, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC
JournalJ Cell Biol
PubMed ID10366597
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 ... More
Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix.
AuthorsMoriyama K, Yahara I
JournalEMBO J
PubMed ID10581248
The biochemical activities of cofilin are controversial. We demonstrated that porcine cofilin severs actin filaments and accelerates monomer release at the pointed ends. At pH 7.1, 0.8 microM cofilin cut filaments (2.2 microM actin) about every 290 subunits and increased the depolymerization rate 6.4-fold. A kink in the major alpha-helix ... More
Control of actin dynamics in cell motility.
AuthorsCarlier MF, Pantaloni D
JournalJ Mol Biol
PubMed ID9217250
Actin polymerization plays a major role in cell movement. The controls of actin sequestration/desequestration and of filament turnover are two important features of cell motility. Actin binding proteins use properties derived from the steady-state monomer-polymer cycle of actin in the presence of ATP, to control the F-actin/G-actin ratio and the ... More
Distribution among tissues and intracellular localization of cofilin, a 21kDa actin-binding protein.
AuthorsYonezawa N, Nishida E, Koyasu S, Maekawa S, Ohta Y, Yahara I, Sakai H
JournalCell Struct Funct
PubMed ID3315240
Cofilin, a 21kDa actin-binding protein, binds to F-actin in a 1:1 molar ratio of cofilin to actin molecule (Nishida, E., S. Maekawa, and H. Sakai, Biochemistry, 23, 5307-5313, 1984) and is capable of controlling actin polymerization and depolymerization in vitro in a pH-sensitive manner (Yonezawa, N., E. Nishida, and H. ... More
Cofilin and DNase I affect the conformation of the small domain of actin.
AuthorsDedova IV, Dedov VN, Nosworthy NJ, Hambly BD, dos Remedios CG
JournalBiophys J
PubMed ID12023237
Cofilin binding induces an allosteric conformational change in subdomain 2 of actin, reducing the distance between probes attached to Gln-41 (subdomain 2) and Cys-374 (subdomain 1) from 34.4 to 31.4 A (pH 6.8) as demonstrated by fluorescence energy transfer spectroscopy. This effect was slightly less pronounced at pH 8.0. In ... More
Electrophoretic monitoring of pollutants: effect of cations and organic compounds on protein interactions monitored by native gel electrophoresis.
AuthorsKekic M, dos Remedios CG
JournalElectrophoresis
PubMed ID10451114
We describe how the interaction between actin and its protein ligands can be used to evaluate the presence of certain metal (Cd, Cu, Hg, Zn) ions and organic compounds (2,4-dioxin or Picloram) which are common components of environmental pollution. The assay detects the high-affinity binding of actin to actin-binding proteins ... More
Reconstitution of actin-based motility of Listeria and Shigella using pure proteins.
Actin polymerization is essential for cell locomotion and is thought to generate the force responsible for cellular protrusions. The Arp2/3 complex is required to stimulate actin assembly at the leading edge in response to signalling. The bacteria Listeria and Shigella bypass the signalling pathway and harness the Arp2/3 complex to ... More
Detection of a sequence involved in actin-binding and phosphoinositide-binding in the N-terminal side of cofilin.
AuthorsKusano K, Abe H, Obinata T
JournalMol Cell Biochem
PubMed ID10098980
Cofilin is an actin-binding protein of low molecular weight which is widely distributed in eukaryotes and is deeply involved in the dynamics of actin assembly in the cytoplasm. The actin-binding ability of cofilin is inhibited by inositol phosphates (PIP2), and the PIP2- and actin-binding site(s) has been localized in residues ... More
DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility.
AuthorsKonzok A, Weber I, Simmeth E, Hacker U, Maniak M, Müller-Taubenberger A
JournalJ Cell Biol
PubMed ID10427097
The 64-kD protein DAip1 from Dictyostelium contains nine WD40-repeats and is homologous to the actin-interacting protein 1, Aip1p, from Saccharomyces cerevisiae, and to related proteins from Caenorhabditis, Physarum, and higher eukaryotes.We show that DAip1 is localized to dynamic regions of the cell cortex that are enriched in filamentous actin: phagocytic ... More
Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms.
AuthorsWeber A
JournalMol Cell Biochem
PubMed ID10098971
Actin binding proteins control actin assembly and disassembly by altering the critical concentration and by changing the kinetics of polymerization. All of these control mechanisms in some way or the other make use of the energy of hydrolysis of actin-bound ATP. Capping of barbed filament ends increases the critical concentration ... More
Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop.
AuthorsOhashi K, Nagata K, Maekawa M, Ishizaki T, Narumiya S, Mizuno K
JournalJ Biol Chem
PubMed ID10652353
LIM-kinase 1 (LIMK1) phosphorylates cofilin, an actin-depolymerizing factor, and regulates actin cytoskeletal reorganization. LIMK1 is activated by the small GTPase Rho and its downstream protein kinase ROCK. We now report the site of phosphorylation of LIMK1 by ROCK. In vitro kinase reaction revealed that the active forms of ROCK phosphorylated ... More
Analogous F-actin binding by cofilin and gelsolin segment 2 substantiates their structural relationship.
AuthorsVan Troys M, Dewitte D, Verschelde JL, Goethals M, Vandekerckhove J, Ampe C
JournalJ Biol Chem
PubMed ID9407048
Cofilin is representative for a family of low molecular weight actin filament binding and depolymerizing proteins. Recently the three-dimensional structure of yeast cofilin and of the cofilin homologs destrin and actophorin were resolved, and a striking similarity to segments of gelsolin and related proteins was observed (Hatanaka, H., Ogura, K., ... More
Cofilin (ADF) affects lateral contacts in F-actin.
AuthorsBobkov AA, Muhlrad A, Shvetsov A, Benchaar S, Scoville D, Almo SC, Reisler E
JournalJ Mol Biol
PubMed ID15001354
The effect of yeast cofilin on lateral contacts between protomers of yeast and skeletal muscle actin filaments was examined in solution. These contacts are presumably stabilized by the interactions of loop 262-274 of one protomer with two other protomers on the opposite strand in F-actin. Cofilin inhibited several-fold the rate ... More
Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides.
AuthorsYonezawa N, Nishida E, Iida K, Yahara I, Sakai H
JournalJ Biol Chem
PubMed ID2160454
Cofilin is a widely distributed actin-modulating protein that has the ability to bind along the side of F-actin and to depolymerize F-actin in a pH-dependent manner. We found that phosphatidylinositol (PI), phosphatidylinositol 4-monophosphate (PIP), and phosphatidylinositol 4,5-bisphosphate (PIP2) inhibited both actions of cofilin in a dose-dependent manner, while inositol 1,4,5-triphosphate ... More
Increased expression of cofilin in dystrophic chicken and mouse skeletal muscles.
AuthorsHayakawa K, Minami N, Ono S, Ogasawara Y, Totsuka T, Abe H, Tanaka T, Obinata T
JournalJ Biochem (Tokyo)
PubMed ID8276772
A monoclonal antibody (McAb) specific for actin depolymerizing factor (ADF) was prepared. With this and previously prepared anti-cofilin McAb (MAB-22) and other antibodies, the expression of cofilin and ADF in the muscles of dystrophic (NH-413) chicken and dystrophic (C57BL/6J dy/dy) mice was compared with that in normal control animals by ... More
Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology.
AuthorsAbe H, Endo T, Yamamoto K, Obinata T
JournalBiochemistry
PubMed ID1699599
Two actin-regulatory proteins of 19 and 20 kDa are involved in the regulation of actin assembly in developing chicken skeletal muscle. They are homologous with actin depolymerizing factor (ADF) and cofilin, a pH-dependent actin-modulating protein, which were originally discovered in chicken and mammalian brain, respectively. In this study, full-length cDNA ... More
Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle.
AuthorsOno S, Minami N, Abe H, Obinata T
JournalJ Biol Chem
PubMed ID8195165
Cofilin is an actin-modulating protein of 20 kDa, which is widely distributed throughout muscle and non-muscle cells. By means of immunoblotting combined with two-dimensional gel electrophoresis, we found that two cofilin variants, muscle type (M-type) and non-muscle type (NM-type), exist in mammals, while a single isoform exists in chickens. During ... More
Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho- and Cdc42-activated LIM-kinase 2.
AuthorsSumi T, Matsumoto K, Takai Y, Nakamura T
JournalJ Cell Biol
PubMed ID10613909
The rapid turnover of actin filaments and the tertiary meshwork formation are regulated by a variety of actin-binding proteins. Protein phosphorylation of cofilin, an actin-binding protein that depolymerizes actin filaments, suppresses its function. Thus, cofilin is a terminal effector of signaling cascades that evokes actin cytoskeletal rearrangement. When wild-type LIMK2 ... More
UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle.
AuthorsOno S, Baillie DL, Benian GM
JournalJ Cell Biol
PubMed ID10225951
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 ... More
Slow axonal transport of soluble actin with actin depolymerizing factor, cofilin, and profilin suggests actin moves in an unassembled form.
AuthorsMills RG, Minamide LS, Yuan A, Bamburg JR, Bray JJ
JournalJ Neurochem
PubMed ID8752130
We examined the axonal transport of actin and its monomer binding proteins, actin depolymerizing factor, cofilin, and profilin, in the chicken sciatic nerve following injection of [35S]methionine into the lumbar spinal cord. At intervals up to 20 days after injection, nerves were cut into 1-cm segments and separated into Triton ... More
A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle.
AuthorsAbe H, Ohshima S, Obinata T
JournalJ Biochem (Tokyo)
PubMed ID2691511
An actin-binding protein of 20 kDa (called 20K protein) was purified from the sarcoplasmic fraction of embryonic chicken skeletal muscle. The properties of this protein were very similar to cofilin, which was discovered in porcine brain (Nishida et al. (1984) Biochemistry, 23, 5307-5313): it bound to both G- and F-actin, ... More
Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics.
AuthorsOno S, Benian GM
JournalJ Biol Chem
PubMed ID9452511
The Caenorhabditis elegans unc-60 gene encodes two actin depolymerizing factor/cofilin proteins which are implicated in the regulation of actin filament assembly in body wall muscle. We examined the interaction of recombinant UNC-60A and B proteins with actin and found that they differentially regulate actin filament dynamics. Co-pelleting assays with F-actin ... More
Cofilin is an essential component of the yeast cortical cytoskeleton.
AuthorsMoon AL, Janmey PA, Louie KA, Drubin DG
JournalJ Cell Biol
PubMed ID8421056
We have biochemically identified the Saccharomyces cerevisiae homologue of the mammalian actin binding protein cofilin. Cofilin and related proteins isolated from diverse organisms are low molecular weight proteins (15-20 kD) that possess several activities in vitro. All bind to monomeric actin and sever filaments, and some can stably associate with ... More
Site-directed mutagenesis of the phosphorylation site of cofilin: its role in cofilin-actin interaction and cytoplasmic localization.
AuthorsNagaoka R, Abe H, Obinata T
JournalCell Motil Cytoskeleton
PubMed ID8913641
It has been demonstrated that the activity of ADF and cofilin, which constitute a functionally related protein family, is markedly altered by phosphorylation, and that the phosphorylation site is Ser 3 in their amino acid sequences [Agnew et al., 1995: J. Biol. Chem. 270:17582-17587; Moriyama et al., 1996: Genes Cells ... More
Essential role of neural Wiskott-Aldrich syndrome protein in neurite extension in PC12 cells and rat hippocampal primary culture cells.
AuthorsBanzai Y, Miki H, Yamaguchi H, Takenawa T
JournalJ Biol Chem
PubMed ID10766829
Neural Wiskott-Aldrich syndrome protein (N-WASP) is an actin-regulating protein that induces filopodium formation downstream of Cdc42. It has been shown that filopodia actively extend from the growth cone, a guidance apparatus located at the tip of neurites, suggesting their role in neurite extension. Here we examined the possible involvement of ... More
Regulation of growth cone actin dynamics by ADF/cofilin.
AuthorsGungabissoon RA, Bamburg JR
JournalJ Histochem Cytochem
PubMed ID12642619
Nervous system development is reliant on neuronal pathfinding, the process in which axons are guided to their target cells by specific extracellular cues. The ability of neurons to extend over long distances in response to environmental guidance signals is made possible by the growth cone, a highly motile structure found ... More
Rapid formation and high diffusibility of actin-cofilin cofilaments at low pH.
AuthorsBonet C, Ternent D, Maciver SK, Mozo-Villarias A
JournalEur J Biochem
PubMed ID10824126
Cofilin is a small actin-binding protein that is known to bind both F-actin and G-actin, severing the former. The interaction of cofilin with actin is pH-sensitive, F-actin being preferentially bound at low pH and G-actin at higher pH, within the physiological range. Diffusion coefficients of F-actin with cofilin were measured ... More
Identification of yeast cofilin residues specific for actin monomer and PIP2 binding.
AuthorsOjala PJ, Paavilainen V, Lappalainen P
JournalBiochemistry
PubMed ID11747431
Cofilin/ADF is a ubiquitous actin-binding protein that is important for rapid actin dynamics in vivo. The long alpha-helix (helix 3 in yeast cofilin) forms the most highly conserved region in cofilin/ADF proteins, and residues in the NH2-terminal half of this alpha-helix have been shown to be essential for actin binding ... More
Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin.
AuthorsNishida E, Maekawa S, Sakai H
JournalBiochemistry
PubMed ID6509022
Cofilin, a 21 000 molecular weight protein of porcine brain, reacts stoichiometrically with actin in a 1:1 molar ratio. Upon binding of cofilin, the fluorescence of pyrene-labeled actin under polymerizing conditions is changed into the monomer form, irrespective of whether cofilin is added to actin before or after polymerization. Cofilin ... More
Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis.
AuthorsGunsalus KC, Bonaccorsi S, Williams E, Verni F, Gatti M, Goldberg ML
JournalJ Cell Biol
PubMed ID8522587
We describe the phenotypic and molecular characterization of twinstar (tsr), an essential gene in Drosophila melanogaster. Two P-element induced alleles of tsr (tsr1 and tsr2) result in late larval or pupal lethality. Cytological examination of actively dividing tissues in these mutants reveals defects in cytokinesis in both mitotic (larval neuroblast) ... More
Signaling pathways involved in dephosphorylation and localization of the actin-binding protein cofilin in stimulated human neutrophils.
AuthorsDjafarzadeh S, Niggli V
JournalExp Cell Res
PubMed ID9367627
We have studied activation-induced dephosphorylation of proteins in human neutrophils loaded with [32P]orthophosphate using two-dimensional gel electrophoresis and autoradiography. A major phosphoprotein of 20 kDa in resting neutrophils was markedly dephosphorylated upon activation of cells with chemotactic peptide or phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C (PKC). ... More
Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails.
In contrast to the slow rate of depolymerization of pure actin in vitro, populations of actin filaments in vivo turn over rapidly. Therefore, the rate of actin depolymerization must be accelerated by one or more factors in the cell. Since the actin dynamics in Listeria monocytogenes tails bear many similarities ... More
Characterization and identification as cofilin and destrin of two thyrotropin- and phorbol ester-regulated phosphoproteins in thyroid cells.
AuthorsSaito T, Lamy F, Roger PP, Lecocq R, Dumont JE
JournalExp Cell Res
PubMed ID8174642
Using separation of total cellular proteins by two dimensional (2-D) gel electrophoresis (isoelectric focusing/SDS-PAGE) we have characterized two regulated proteins, p21 and p19, in dog thyroid cells. We have used the same 2-D gel technique to purify these proteins before their trypsin cleavage and partial sequencing. Three peptides were sequenced ... More
Quantitative analysis of low molecular weight G-actin-binding proteins, cofilin, ADF and profilin, expressed in developing and degenerating chicken skeletal muscles.
AuthorsNagaoka R, Minami N, Hayakawa K, Abe H, Obinata T
JournalJ Muscle Res Cell Motil
PubMed ID8884601
A large amount of G-actin is pooled in the cytoplasm of young embryonic skeletal muscle and, although its concentration is reduced as muscle develops, the total amount of actin in muscle cells increases remarkably. Three G-actin-binding proteins, cofilin, ADF and profilin, are known to be involved in creating the G-actin ... More
Structural effects of cofilin on longitudinal contacts in F-actin.
AuthorsBobkov AA, Muhlrad A, Kokabi K, Vorobiev S, Almo SC, Reisler E
JournalJ Mol Biol
PubMed ID12419261
Structural effects of yeast cofilin on skeletal muscle and yeast actin were examined in solution. Cofilin binding to native actin was non-cooperative and saturated at a 1:1 molar ratio, with K(d)<or=0.05 microM for both CaATP-G-actin and F-actin. Cofilin binding enhanced the fluorescence of dansyl ethylenediamine (DED) attached to Gln41 on ... More
A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain.
AuthorsDevineni N, Minamide LS, Niu M, Safer D, Verma R, Bamburg JR, Nachmias VT
JournalBrain Res
PubMed ID10095019
The large G-actin pool in individual actively motile cells has been shown to be maintained primarily by the actin sequestering protein thymosin beta four (Tbeta4). It is not clear whether Tbeta4 or an isoform also plays a primary role in neural tissue containing highly motile axonal growth cones. To address ... More
Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action.
AuthorsNagaoka R, Kusano K, Abe H, Obinata T
JournalJ Cell Sci
PubMed ID7769003
The previous investigation (Abe et al. (1989) J. Biochem. 106, 696-702) suggested that cofilin is deeply involved in the regulation of actin assembly in developing skeletal muscle. In this study, to examine further the function of cofilin in living myogenic cells in culture, recombinant cofilin having extra Cys residues at ... More