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Volumn 68, Issue 9, 2011, Pages 471-490

Actin-depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics

Author keywords

Actin; Actin binding protein 1; Actin depolymerizing factor cofilin; Coactosin; Drebrin; Glia maturation factor; Twinfilin

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN DEPOLYMERIZING FACTOR; COFILIN; CYTOSKELETON PROTEIN; DREBRIN; GLIA MATURATION FACTOR;

EID: 80052990415     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20530     Document Type: Review
Times cited : (123)

References (226)
  • 2
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew BJ, Minamide LS, Bamburg JR. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J Biol Chem 270: 17582-17587.
    • (1995) J Biol Chem , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 4
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro E, Pollard TD. 2006. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell 24: 13-23.
    • (2006) Mol Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 6
    • 44349105297 scopus 로고    scopus 로고
    • Actin depolymerizing factor is essential for viability in plants, and its phosphoregulation is important for tip growth
    • Augustine RC, Vidali L, Kleinman KP, Bezanilla M. 2008. Actin depolymerizing factor is essential for viability in plants, and its phosphoregulation is important for tip growth. Plant J 54: 863-875.
    • (2008) Plant J , vol.54 , pp. 863-875
    • Augustine, R.C.1    Vidali, L.2    Kleinman, K.P.3    Bezanilla, M.4
  • 7
    • 0347664159 scopus 로고    scopus 로고
    • Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1
    • Balcer HI, Goodman AL, Rodal AA, Smith E, Kugler J, Heuser JE, Goode BL. 2003. Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1. Curr Biol 13: 2159-2169.
    • (2003) Curr Biol , vol.13 , pp. 2159-2169
    • Balcer, H.I.1    Goodman, A.L.2    Rodal, A.A.3    Smith, E.4    Kugler, J.5    Heuser, J.E.6    Goode, B.L.7
  • 8
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: essential regulators of actin dynamics
    • Bamburg JR. 1999. Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15: 185-230.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 9
    • 0019170917 scopus 로고
    • Partial purification and characterization of an actin depolymerizing factor from brain
    • Bamburg JR, Harris HE, Weeds AG. 1980. Partial purification and characterization of an actin depolymerizing factor from brain. FEBS Lett 121: 178-182.
    • (1980) FEBS Lett , vol.121 , pp. 178-182
    • Bamburg, J.R.1    Harris, H.E.2    Weeds, A.G.3
  • 11
    • 34548850904 scopus 로고    scopus 로고
    • N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex
    • Bellenchi GC, Gurniak CB, Perlas E, Middei S, Ammassari-Teule M, Witke W. 2007. N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex. Genes Dev 21: 2347-2357.
    • (2007) Genes Dev , vol.21 , pp. 2347-2357
    • Bellenchi, G.C.1    Gurniak, C.B.2    Perlas, E.3    Middei, S.4    Ammassari-Teule, M.5    Witke, W.6
  • 13
    • 77955615646 scopus 로고    scopus 로고
    • Mathematical modeling of endocytic actin patch kinetics in fission yeast: disassembly requires release of actin filament fragments
    • Berro J, Sirotkin V, Pollard TD. 2010. Mathematical modeling of endocytic actin patch kinetics in fission yeast: disassembly requires release of actin filament fragments. Mol Biol Cell 21: 2905-2915.
    • (2010) Mol Biol Cell , vol.21 , pp. 2905-2915
    • Berro, J.1    Sirotkin, V.2    Pollard, T.D.3
  • 14
    • 0034710563 scopus 로고    scopus 로고
    • A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast
    • Baum B, Li W, Perrimon N. 2000. A cyclase-associated protein regulates actin and cell polarity during Drosophila oogenesis and in yeast. Curr Biol 10: 964-973.
    • (2000) Curr Biol , vol.10 , pp. 964-973
    • Baum, B.1    Li, W.2    Perrimon, N.3
  • 16
    • 0030740478 scopus 로고    scopus 로고
    • Cloning and characterization of the mouse homolog of the human A6 gene
    • Beeler JF, Patel BK, Chedid M, LaRochelle WJ. 1997. Cloning and characterization of the mouse homolog of the human A6 gene. Gene 193: 31-37.
    • (1997) Gene , vol.193 , pp. 31-37
    • Beeler, J.F.1    Patel, B.K.2    Chedid, M.3    LaRochelle, W.J.4
  • 17
    • 34548850904 scopus 로고    scopus 로고
    • N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex
    • Bellenchi GC, Gurniak CB, Perlas E, Middei S, Ammassari-Teule M, Witke W. 2007. N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex. Genes Dev 21: 2347-2357.
    • (2007) Genes Dev , vol.21 , pp. 2347-2357
    • Bellenchi, G.C.1    Gurniak, C.B.2    Perlas, E.3    Middei, S.4    Ammassari-Teule, M.5    Witke, W.6
  • 18
    • 0034724535 scopus 로고    scopus 로고
    • Act up controls actin polymerization to alter cell shape and restrict Hedgehog signaling in the Drosophila eye disc
    • Benlali A, Draskovic I, Hazelett DJ, Treisman JE. 2000. Act up controls actin polymerization to alter cell shape and restrict Hedgehog signaling in the Drosophila eye disc. Cell 101: 271-281.
    • (2000) Cell , vol.101 , pp. 271-281
    • Benlali, A.1    Draskovic, I.2    Hazelett, D.J.3    Treisman, J.E.4
  • 19
    • 77950859278 scopus 로고    scopus 로고
    • ADF/cofilin: a functional node in cell biology
    • Bernstein BW, Bamburg JR. 2010. ADF/cofilin: a functional node in cell biology. Trends Cell Biol 20: 187-195.
    • (2010) Trends Cell Biol , vol.20 , pp. 187-195
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 20
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells
    • Bertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, Lappalainen P. 2004. Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Mol Biol Cell 15: 2324-2334.
    • (2004) Mol Biol Cell , vol.15 , pp. 2324-2334
    • Bertling, E.1    Hotulainen, P.2    Mattila, P.K.3    Matilainen, T.4    Salminen, M.5    Lappalainen, P.6
  • 22
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L, Pollard TD. 1998. Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin. J Biol Chem 273: 25106-25111.
    • (1998) J Biol Chem , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 23
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • Blanchoin L, Pollard TD, Mullins RD. 2000a. Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr Biol 10: 1273-1282.
    • (2000) Curr Biol , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 24
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • Blanchoin L, Robinson RC, Choe S, Pollard TD. 2000b. Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure. J Mol Biol 295: 203-211.
    • (2000) J Mol Biol , vol.295 , pp. 203-211
    • Blanchoin, L.1    Robinson, R.C.2    Choe, S.3    Pollard, T.D.4
  • 25
    • 30744462047 scopus 로고    scopus 로고
    • Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function
    • Bobkov AA, Muhlrad A, Pavlov DA, Kokabi K, Yilmaz A, Reisler E. 2006. Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function. J Mol Biol 356: 325-334.
    • (2006) J Mol Biol , vol.356 , pp. 325-334
    • Bobkov, A.A.1    Muhlrad, A.2    Pavlov, D.A.3    Kokabi, K.4    Yilmaz, A.5    Reisler, E.6
  • 26
    • 0024429369 scopus 로고
    • Axonal signals regulate expression of glia maturation factor-beta in Schwann cells: an immunohistochemical study of injured sciatic nerves and cultured Schwann cells
    • Bosch EP, Zhong W, Lim R. 1989. Axonal signals regulate expression of glia maturation factor-beta in Schwann cells: an immunohistochemical study of injured sciatic nerves and cultured Schwann cells. J Neurosci 9: 3690-3698.
    • (1989) J Neurosci , vol.9 , pp. 3690-3698
    • Bosch, E.P.1    Zhong, W.2    Lim, R.3
  • 27
    • 33750365532 scopus 로고    scopus 로고
    • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1
    • Brieher WM, Kueh HY, Ballif BA, Mitchison TJ. 2006. Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. J Cell Biol 175: 315-324.
    • (2006) J Cell Biol , vol.175 , pp. 315-324
    • Brieher, W.M.1    Kueh, H.Y.2    Ballif, B.A.3    Mitchison, T.J.4
  • 29
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi B, Carlier MF. 2010. Control of actin filament treadmilling in cell motility. Annu Rev Biophys 39: 449-470.
    • (2010) Annu Rev Biophys , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.F.2
  • 30
    • 33847420825 scopus 로고    scopus 로고
    • Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge
    • Cai L, Marshall TW, Uetrecht AC, Schafer DA, Bear JE. 2007. Coronin 1B coordinates Arp2/3 complex and cofilin activities at the leading edge. Cell 128: 915-929.
    • (2007) Cell , vol.128 , pp. 915-929
    • Cai, L.1    Marshall, T.W.2    Uetrecht, A.C.3    Schafer, D.A.4    Bear, J.E.5
  • 33
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • Chan C, Beltzner CC, Pollard TD. 2009. Cofilin dissociates Arp2/3 complex and branches from actin filaments. Curr Biol 19: 537-545.
    • (2009) Curr Biol , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 34
    • 77951917756 scopus 로고    scopus 로고
    • A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo
    • Chaudhry F, Little K, Talarico L, Quintero-Monzon O, Goode BL. 2010. A central role for the WH2 domain of Srv2/CAP in recharging actin monomers to drive actin turnover in vitro and in vivo. Cytoskeleton (Hoboken) 67: 120-133.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 120-133
    • Chaudhry, F.1    Little, K.2    Talarico, L.3    Quintero-Monzon, O.4    Goode, B.L.5
  • 35
    • 0035153556 scopus 로고    scopus 로고
    • Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis
    • Chen J, Godt D, Gunsalus K, Kiss I, Goldberg M, Laski FA. 2001. Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis. Nat Cell Biol. 3: 204-209.
    • (2001) Nat Cell Biol. , vol.3 , pp. 204-209
    • Chen, J.1    Godt, D.2    Gunsalus, K.3    Kiss, I.4    Goldberg, M.5    Laski, F.A.6
  • 36
    • 2642580847 scopus 로고    scopus 로고
    • In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups
    • Chen H, Bernstein BW, Sneider JM, Boyle JA, Minamide LS, Bamburg JR. 2004. In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups. Biochemistry 43: 7127-7142.
    • (2004) Biochemistry , vol.43 , pp. 7127-7142
    • Chen, H.1    Bernstein, B.W.2    Sneider, J.M.3    Boyle, J.A.4    Minamide, L.S.5    Bamburg, J.R.6
  • 37
    • 59249107059 scopus 로고    scopus 로고
    • Immunoscreening of urinary bladder cancer cDNA library and identification of potential tumor antigen
    • Chen L, Chen W, Zhao L, Yu HZ, Li X. 2009. Immunoscreening of urinary bladder cancer cDNA library and identification of potential tumor antigen. World J Urol 27: 107-112.
    • (2009) World J Urol , vol.27 , pp. 107-112
    • Chen, L.1    Chen, W.2    Zhao, L.3    Yu, H.Z.4    Li, X.5
  • 38
    • 0033983608 scopus 로고    scopus 로고
    • Non-muscle myosin IIB-like immunoreactivity is present at the drebrin-binding cytoskeleton in neurons
    • Cheng XT, Hayashi K, Shirao T. 2000. Non-muscle myosin IIB-like immunoreactivity is present at the drebrin-binding cytoskeleton in neurons. Neurosci Res 36: 167-173.
    • (2000) Neurosci Res , vol.36 , pp. 167-173
    • Cheng, X.T.1    Hayashi, K.2    Shirao, T.3
  • 39
    • 0344668558 scopus 로고    scopus 로고
    • Mitochondrial translocation of cofilin is an early step in apoptosis induction
    • Chua BT, Volbracht C, Tan KO, Li R, Yu VC, Li P. 2003. Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nat Cell Biol 5: 1083-1089.
    • (2003) Nat Cell Biol , vol.5 , pp. 1083-1089
    • Chua, B.T.1    Volbracht, C.2    Tan, K.O.3    Li, R.4    Yu, V.C.5    Li, P.6
  • 40
    • 77957834345 scopus 로고    scopus 로고
    • Differential regulation of unconventional fission yeast myosins via the actin track
    • Clayton JE, Sammons MR, Stark BC, Hodges AR, and Lord M. 2010. Differential regulation of unconventional fission yeast myosins via the actin track. Curr Biol 20: 1423-1431.
    • (2010) Curr Biol , vol.20 , pp. 1423-1431
    • Clayton, J.E.1    Sammons, M.R.2    Stark, B.C.3    Hodges, A.R.4    Lord, M.5
  • 42
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-dalton actin-binding protein from Acanthamoeba castellanii
    • Cooper JA, Blum JD, Williams RC Jr., Pollard TD. 1986. Purification and characterization of actophorin, a new 15, 000-dalton actin-binding protein from Acanthamoeba castellanii. J Biol Chem 261: 477-485.
    • (1986) J Biol Chem , vol.261 , pp. 477-485
    • Cooper, J.A.1    Blum, J.D.2    Williams Jr., R.C.3    Pollard, T.D.4
  • 43
    • 0033594087 scopus 로고    scopus 로고
    • Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast
    • Cope MJ, Yang S, Shang C, Drubin DG. 1999. Novel protein kinases Ark1p and Prk1p associate with and regulate the cortical actin cytoskeleton in budding yeast. J Cell Biol 144: 1203-1218.
    • (1999) J Cell Biol , vol.144 , pp. 1203-1218
    • Cope, M.J.1    Yang, S.2    Shang, C.3    Drubin, D.G.4
  • 44
    • 26444593474 scopus 로고    scopus 로고
    • Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae
    • D'Agostino JL, Goode BL. 2005. Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae. Genetics 171: 35-47.
    • (2005) Genetics , vol.171 , pp. 35-47
    • D'Agostino, J.L.1    Goode, B.L.2
  • 47
    • 77950022821 scopus 로고    scopus 로고
    • How cofilin severs an actin filament
    • De La Cruz EM. 2009. How cofilin severs an actin filament. Biophys Rev 1: 51-59.
    • (2009) Biophys Rev , vol.1 , pp. 51-59
    • De La Cruz, E.M.1
  • 48
    • 3042546532 scopus 로고    scopus 로고
    • Two opposite effects of cofilin on the thermal unfolding of F-actin: a differential scanning calorimetric study
    • Dedova IV, Nikolaeva OP, Mikhailova VV, dos Remedios CG, Levitsky DI. 2004. Two opposite effects of cofilin on the thermal unfolding of F-actin: a differential scanning calorimetric study. Biophys Chem 110: 119-128.
    • (2004) Biophys Chem , vol.110 , pp. 119-128
    • Dedova, I.V.1    Nikolaeva, O.P.2    Mikhailova, V.V.3    dos Remedios, C.G.4    Levitsky, D.I.5
  • 51
    • 6344228185 scopus 로고    scopus 로고
    • Actin-binding proteins-a unifying hypothesis
    • Dominguez R. 2004. Actin-binding proteins-a unifying hypothesis. Trends Biochem Sci 29: 572-578.
    • (2004) Trends Biochem Sci , vol.29 , pp. 572-578
    • Dominguez, R.1
  • 52
    • 0036297769 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of mouse coactosin-like protein
    • Doucet J, Provost P, Samuelsson B, Radmark O. 2002. Molecular cloning and functional characterization of mouse coactosin-like protein. Biochem Biophys Res Commun 290: 783-789.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 783-789
    • Doucet, J.1    Provost, P.2    Samuelsson, B.3    Radmark, O.4
  • 53
    • 0024192883 scopus 로고
    • Yeast actin-binding proteins: evidence for a role in morphogenesis
    • Drubin DG, Miller KG, Botstein D. 1988. Yeast actin-binding proteins: evidence for a role in morphogenesis. J Cell Biol 107: 2551-2561.
    • (1988) J Cell Biol , vol.107 , pp. 2551-2561
    • Drubin, D.G.1    Miller, K.G.2    Botstein, D.3
  • 54
    • 77950271947 scopus 로고    scopus 로고
    • Control of cell shape and plasticity during development and disease by the actin-binding protein Drebrin
    • Dun XP, Chilton JK. 2010. Control of cell shape and plasticity during development and disease by the actin-binding protein Drebrin. Histol Histopathol 25: 533-540.
    • (2010) Histol Histopathol , vol.25 , pp. 533-540
    • Dun, X.P.1    Chilton, J.K.2
  • 55
    • 0033607769 scopus 로고    scopus 로고
    • A novel src homology 3 domain-containing adaptor protein, HIP-55, that interacts with hematopoietic progenitor kinase 1
    • Ensenat D, Yao Z, Wang XS, Kori R, Zhou G, Lee SC, Tan TH. 1999. A novel src homology 3 domain-containing adaptor protein, HIP-55, that interacts with hematopoietic progenitor kinase 1. J Biol Chem 274: 33945-33950.
    • (1999) J Biol Chem , vol.274 , pp. 33945-33950
    • Ensenat, D.1    Yao, Z.2    Wang, X.S.3    Kori, R.4    Zhou, G.5    Lee, S.C.6    Tan, T.H.7
  • 59
    • 0038504029 scopus 로고    scopus 로고
    • Interactions between Piccolo and the actin/dynamin-binding protein Abp1 link vesicle endocytosis to presynaptic active zones
    • Fenster SD, Kessels MM, Qualmann B, Chung WJ, Nash J, Gundelfinger ED, Garner CC. 2003. Interactions between Piccolo and the actin/dynamin-binding protein Abp1 link vesicle endocytosis to presynaptic active zones. J Biol Chem 278: 20268-20277.
    • (2003) J Biol Chem , vol.278 , pp. 20268-20277
    • Fenster, S.D.1    Kessels, M.M.2    Qualmann, B.3    Chung, W.J.4    Nash, J.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 60
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • Galkin VE, Orlova A, Lukoyanova N, Wriggers W, Egelman EH. 2001. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol 153: 75-86.
    • (2001) J Cell Biol , vol.153 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggers, W.4    Egelman, E.H.5
  • 61
    • 65549103882 scopus 로고    scopus 로고
    • Coronin switches roles in actin disassembly depending on the nucleotide state of actin
    • Gandhi M, Achard V, Blanchoin L, Goode BL. 2009. Coronin switches roles in actin disassembly depending on the nucleotide state of actin. Mol Cell 34: 364-374.
    • (2009) Mol Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Achard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 62
    • 78049414514 scopus 로고    scopus 로고
    • Functional surfaces on the actin-binding protein coronin revealed by systematic mutagenesis
    • Gandhi M, Jangi M, Goode BL. 2010a. Functional surfaces on the actin-binding protein coronin revealed by systematic mutagenesis. J Biol Chem 285: 34899-34908.
    • (2010) J Biol Chem , vol.285 , pp. 34899-34908
    • Gandhi, M.1    Jangi, M.2    Goode, B.L.3
  • 64
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla A, Birkenfeld J, Bokoch GM. 2005. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7: 21-29.
    • (2005) Nat Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 65
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • Goley ED, Welch MD. 2006. The ARP2/3 complex: an actin nucleator comes of age. Nat Rev Mol Cell Biol 7: 713-726.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 66
    • 0031828002 scopus 로고    scopus 로고
    • Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein
    • Goode BL, Drubin DG, Lappalainen P. 1998. Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J Cell Biol 142: 723-733.
    • (1998) J Cell Biol , vol.142 , pp. 723-733
    • Goode, B.L.1    Drubin, D.G.2    Lappalainen, P.3
  • 67
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode BL, Rodal AA, Barnes G, Drubin DG. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J Cell Biol 153: 627-634.
    • (2001) J Cell Biol , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 70
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning P, O'Neill G, Hardeman E. 2008. Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol Rev 88: 1-35.
    • (2008) Physiol Rev , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 71
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • Gunsalus KC, Bonaccorsi S, Williams E, Verni F, Gatti M, Goldberg ML. 1995. Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis. J Cell Biol 131: 1243-1259.
    • (1995) J Cell Biol , vol.131 , pp. 1243-1259
    • Gunsalus, K.C.1    Bonaccorsi, S.2    Williams, E.3    Verni, F.4    Gatti, M.5    Goldberg, M.L.6
  • 72
    • 11844276055 scopus 로고    scopus 로고
    • The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration
    • Gurniak CB, Perlas E, Witke W. 2005. The actin depolymerizing factor n-cofilin is essential for neural tube morphogenesis and neural crest cell migration. Dev Biol 278: 231-241.
    • (2005) Dev Biol , vol.278 , pp. 231-241
    • Gurniak, C.B.1    Perlas, E.2    Witke, W.3
  • 73
    • 54049138871 scopus 로고    scopus 로고
    • The actin-binding protein Abp1 controls dendritic spine morphology and is important for spine head and synapse formation
    • Haeckel A, Ahuja R, Gundelfinger ED, Qualmann B, Kessels MM. 2008. The actin-binding protein Abp1 controls dendritic spine morphology and is important for spine head and synapse formation. J Neurosci 28: 10031-10044.
    • (2008) J Neurosci , vol.28 , pp. 10031-10044
    • Haeckel, A.1    Ahuja, R.2    Gundelfinger, E.D.3    Qualmann, B.4    Kessels, M.M.5
  • 74
    • 0347362831 scopus 로고    scopus 로고
    • The SH3 domain-containing adaptor HIP-55 mediates c-Jun N-terminal kinase activation in T cell receptor signaling
    • Han J, Kori R, Shui JW, Chen YR, Yao Z, Tan TH. 2003. The SH3 domain-containing adaptor HIP-55 mediates c-Jun N-terminal kinase activation in T cell receptor signaling. J Biol Chem 278: 52195-52202.
    • (2003) J Biol Chem , vol.278 , pp. 52195-52202
    • Han, J.1    Kori, R.2    Shui, J.W.3    Chen, Y.R.4    Yao, Z.5    Tan, T.H.6
  • 76
    • 0030025216 scopus 로고    scopus 로고
    • Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease
    • Harigaya Y, Shoji M, Shirao T, Hirai S. 1996. Disappearance of actin-binding protein, drebrin, from hippocampal synapses in Alzheimer's disease. J Neurosci Res 43: 87-92.
    • (1996) J Neurosci Res , vol.43 , pp. 87-92
    • Harigaya, Y.1    Shoji, M.2    Shirao, T.3    Hirai, S.4
  • 77
    • 0030604703 scopus 로고    scopus 로고
    • Tertiary structure of destrin and structural similarity between two actin-regulating protein families
    • Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F. 1996. Tertiary structure of destrin and structural similarity between two actin-regulating protein families. Cell 85: 1047-1055.
    • (1996) Cell , vol.85 , pp. 1047-1055
    • Hatanaka, H.1    Ogura, K.2    Moriyama, K.3    Ichikawa, S.4    Yahara, I.5    Inagaki, F.6
  • 78
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M, Pope B, Maciver SK, Weeds AG. 1993. Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32: 9985-9993.
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 79
    • 0033562792 scopus 로고    scopus 로고
    • Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons
    • Hayashi K, Shirao T. 1999. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J Neurosci 19: 3918-3925.
    • (1999) J Neurosci , vol.19 , pp. 3918-3925
    • Hayashi, K.1    Shirao, T.2
  • 81
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR. 1993. Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32: 9994-10004.
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 83
  • 85
    • 0027244817 scopus 로고
    • Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae
    • Holtzman DA, Yang S, Drubin DG. 1993. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J Cell Biol 122: 635-644.
    • (1993) J Cell Biol , vol.122 , pp. 635-644
    • Holtzman, D.A.1    Yang, S.2    Drubin, D.G.3
  • 86
    • 12844269159 scopus 로고    scopus 로고
    • Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • Hotulainen P, Paunola E, Vartiainen MK, Lappalainen P. 2005. Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol Biol Cell 16: 649-664.
    • (2005) Mol Biol Cell , vol.16 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartiainen, M.K.3    Lappalainen, P.4
  • 87
    • 70849133453 scopus 로고    scopus 로고
    • Expression of chick Coactosin in cells in morphogenetic movement
    • Hou X, Katahira T, Kimura J, Nakamura H. 2009. Expression of chick Coactosin in cells in morphogenetic movement. Dev Growth Differ 51: 833-840.
    • (2009) Dev Growth Differ , vol.51 , pp. 833-840
    • Hou, X.1    Katahira, T.2    Kimura, J.3    Nakamura, H.4
  • 88
    • 0037688016 scopus 로고    scopus 로고
    • Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor)
    • Ikeda S, Cunningham LA, Boggess D, Hawes N, Hobson CD, Sundberg JP, Naggert JK, Smith RS, Nishina PM. 2003. Aberrant actin cytoskeleton leads to accelerated proliferation of corneal epithelial cells in mice deficient for destrin (actin depolymerizing factor). Hum Mol Genet 12: 1029-1037.
    • (2003) Hum Mol Genet , vol.12 , pp. 1029-1037
    • Ikeda, S.1    Cunningham, L.A.2    Boggess, D.3    Hawes, N.4    Hobson, C.D.5    Sundberg, J.P.6    Naggert, J.K.7    Smith, R.S.8    Nishina, P.M.9
  • 89
    • 33747390456 scopus 로고    scopus 로고
    • Glia maturation factor-gamma is preferentially expressed in microvascular endothelial and inflammatory cells and modulates actin cytoskeleton reorganization
    • Ikeda K, Kundu RK, Ikeda S, Kobara M, Matsubara H, Quertermous T. 2006. Glia maturation factor-gamma is preferentially expressed in microvascular endothelial and inflammatory cells and modulates actin cytoskeleton reorganization. Circ Res 99: 424-433.
    • (2006) Circ Res , vol.99 , pp. 424-433
    • Ikeda, K.1    Kundu, R.K.2    Ikeda, S.3    Kobara, M.4    Matsubara, H.5    Quertermous, T.6
  • 90
    • 0019256032 scopus 로고
    • An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions
    • Isenberg G, Aebi U, Pollard TD. 1980. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 288: 455-459.
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.1    Aebi, U.2    Pollard, T.D.3
  • 91
    • 0028139040 scopus 로고
    • Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments
    • Ishikawa R, Hayashi K, Shirao T, Xue Y, Takagi T, Sasaki Y, Kohama K. 1994. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J Biol Chem 269: 29928-29933.
    • (1994) J Biol Chem , vol.269 , pp. 29928-29933
    • Ishikawa, R.1    Hayashi, K.2    Shirao, T.3    Xue, Y.4    Takagi, T.5    Sasaki, Y.6    Kohama, K.7
  • 93
    • 77955893542 scopus 로고    scopus 로고
    • Genetic evidence for concerted control of actin dynamics in cytokinesis, endocytic traffic, and cell motility by coronin and Aip1
    • Ishikawa-Ankerhold HC, Gerisch G, Müller-Taubenberger A. 2010. Genetic evidence for concerted control of actin dynamics in cytokinesis, endocytic traffic, and cell motility by coronin and Aip1. Cytoskeleton (Hoboken) 67: 442-455.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 442-455
    • Ishikawa-Ankerhold, H.C.1    Gerisch, G.2    Müller-Taubenberger, A.3
  • 94
    • 79951531654 scopus 로고    scopus 로고
    • Proteomic analysis of human small cell lung cancer tissues: up-regulation of coactosin-like protein-1
    • Jeong HC, Kim GI, Cho SH, Lee KH, Ko JJ, Yang JH, Chung KH. 2011. Proteomic analysis of human small cell lung cancer tissues: up-regulation of coactosin-like protein-1. J Proteome Res 10: 269-276.
    • (2011) J Proteome Res , vol.10 , pp. 269-276
    • Jeong, H.C.1    Kim, G.I.2    Cho, S.H.3    Lee, K.H.4    Ko, J.J.5    Yang, J.H.6    Chung, K.H.7
  • 95
    • 0036247552 scopus 로고    scopus 로고
    • A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping, genomic structure, expression, and functional characterization
    • Jin M, Tanaka S, Sekino Y, Ren Y, Yamazaki H, Kawai-Hirai R, Kojima N, Shirao T. 2002. A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal mapping, genomic structure, expression, and functional characterization. Genomics 79: 686-692.
    • (2002) Genomics , vol.79 , pp. 686-692
    • Jin, M.1    Tanaka, S.2    Sekino, Y.3    Ren, Y.4    Yamazaki, H.5    Kawai-Hirai, R.6    Kojima, N.7    Shirao, T.8
  • 96
    • 66749139515 scopus 로고    scopus 로고
    • Polymorphisms of COTL1 gene identified by proteomic approach and their association with autoimmune disorders
    • Jin EH, Shim SC, Kim HG, Chae SC, Chung HT. 2009. Polymorphisms of COTL1 gene identified by proteomic approach and their association with autoimmune disorders. Exp Mol Med 41: 354-361.
    • (2009) Exp Mol Med , vol.41 , pp. 354-361
    • Jin, E.H.1    Shim, S.C.2    Kim, H.G.3    Chae, S.C.4    Chung, H.T.5
  • 97
    • 0041856141 scopus 로고    scopus 로고
    • Induction of glia maturation factor-beta in proximal tubular cells leads to vulnerability to oxidative injury through the p38 pathway and changes in antioxidant enzyme activities
    • Kaimori JY, Takenaka M, Nakajima H, Hamano T, Horio M, Sugaya T, Ito T, Hori M, Okubo K, Imai E. 2003. Induction of glia maturation factor-beta in proximal tubular cells leads to vulnerability to oxidative injury through the p38 pathway and changes in antioxidant enzyme activities. J Biol Chem 278: 33519-33527.
    • (2003) J Biol Chem , vol.278 , pp. 33519-33527
    • Kaimori, J.Y.1    Takenaka, M.2    Nakajima, H.3    Hamano, T.4    Horio, M.5    Sugaya, T.6    Ito, T.7    Hori, M.8    Okubo, K.9    Imai, E.10
  • 98
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, actin during endocytic internalization
    • Kaksonen M, Sun Y, Drubin DG. 2003. A pathway for association of receptors, adaptors, actin during endocytic internalization. Cell 115: 475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 99
    • 0033980106 scopus 로고    scopus 로고
    • Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation
    • Kessels MM, Engqvist-Goldstein AE, Drubin DG. 2000. Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol Biol Cell 11: 393-412.
    • (2000) Mol Biol Cell , vol.11 , pp. 393-412
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.2    Drubin, D.G.3
  • 100
    • 0035897420 scopus 로고    scopus 로고
    • Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin
    • Kessels MM, Engqvist-Goldstein AE, Drubin DG, Qualmann B. 2001. Mammalian Abp1, a signal-responsive F-actin-binding protein, links the actin cytoskeleton to endocytosis via the GTPase dynamin. J Cell Biol 153: 351-366.
    • (2001) J Cell Biol , vol.153 , pp. 351-366
    • Kessels, M.M.1    Engqvist-Goldstein, A.E.2    Drubin, D.G.3    Qualmann, B.4
  • 101
    • 1142277951 scopus 로고    scopus 로고
    • The actin-interacting protein AIP1 is essential for actin organization and plant development
    • Ketelaar T, Allwood EG, Anthony R, Voigt B, Menzel D, Hussey PJ. 2004. The actin-interacting protein AIP1 is essential for actin organization and plant development. Curr Biol 14: 145-149.
    • (2004) Curr Biol , vol.14 , pp. 145-149
    • Ketelaar, T.1    Allwood, E.G.2    Anthony, R.3    Voigt, B.4    Menzel, D.5    Hussey, P.J.6
  • 102
    • 0027353586 scopus 로고
    • Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor
    • Kim SR, Kim Y, An G. 1993. Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor. Plant Mol Biol 21: 39-45.
    • (1993) Plant Mol Biol , vol.21 , pp. 39-45
    • Kim, S.R.1    Kim, Y.2    An, G.3
  • 103
    • 34248227301 scopus 로고    scopus 로고
    • Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers
    • Kiuchi T, Ohashi K, Kurita S, Mizuno K. 2007. Cofilin promotes stimulus-induced lamellipodium formation by generating an abundant supply of actin monomers. J Cell Biol 177: 465-476.
    • (2007) J Cell Biol , vol.177 , pp. 465-476
    • Kiuchi, T.1    Ohashi, K.2    Kurita, S.3    Mizuno, K.4
  • 105
    • 70449632127 scopus 로고    scopus 로고
    • Genetic disruption of the alternative splicing of drebrin gene impairs context-dependent fear learning in adulthood
    • Kojima N, Hanamura K, Yamazaki H, Ikeda T, Itohara S, Shirao T. 2010. Genetic disruption of the alternative splicing of drebrin gene impairs context-dependent fear learning in adulthood. Neuroscience 165: 138-150.
    • (2010) Neuroscience , vol.165 , pp. 138-150
    • Kojima, N.1    Hanamura, K.2    Yamazaki, H.3    Ikeda, T.4    Itohara, S.5    Shirao, T.6
  • 110
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen P, Drubin DG. 1997. Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 111
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG. 1997. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J 16: 5520-5530.
    • (1997) EMBO J , vol.16 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 112
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: a highly exploited actin-binding module
    • Lappalainen P, Kessels MM, Cope MJ, Drubin DG. 1998. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Mol Biol Cell 9: 1951-1959.
    • (1998) Mol Biol Cell , vol.9 , pp. 1951-1959
    • Lappalainen, P.1    Kessels, M.M.2    Cope, M.J.3    Drubin, D.G.4
  • 113
    • 0032952693 scopus 로고    scopus 로고
    • SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors
    • Larbolette O, Wollscheid B, Schweikert J, Nielsen PJ, Wienands J. 1999. SH3P7 is a cytoskeleton adapter protein and is coupled to signal transduction from lymphocyte antigen receptors. Mol Cell Biol 19: 1539-1546.
    • (1999) Mol Cell Biol , vol.19 , pp. 1539-1546
    • Larbolette, O.1    Wollscheid, B.2    Schweikert, J.3    Nielsen, P.J.4    Wienands, J.5
  • 114
    • 2442461214 scopus 로고    scopus 로고
    • Recruitment of the actin-binding protein HIP-55 to the immunological synapse regulates T cell receptor signaling and endocytosis
    • Le Bras S, Foucault I, Foussat A, Brignone C, Acuto O, Deckert M. 2004. Recruitment of the actin-binding protein HIP-55 to the immunological synapse regulates T cell receptor signaling and endocytosis. J Biol Chem 279: 15550-15560.
    • (2004) J Biol Chem , vol.279 , pp. 15550-15560
    • Le Bras, S.1    Foucault, I.2    Foussat, A.3    Brignone, C.4    Acuto, O.5    Deckert, M.6
  • 116
    • 7244236804 scopus 로고    scopus 로고
    • Crystal structure of human coactosin-like protein at 1.9 A resolution
    • Li X, Liu X, Lou Z, Duan X, Wu H, Liu Y, Rao Z. 2004. Crystal structure of human coactosin-like protein at 1.9 A resolution. Protein Sci 13: 2845-2851.
    • (2004) Protein Sci , vol.13 , pp. 2845-2851
    • Li, X.1    Liu, X.2    Lou, Z.3    Duan, X.4    Wu, H.5    Liu, Y.6    Rao, Z.7
  • 117
    • 77954895288 scopus 로고    scopus 로고
    • Attenuation of microRNA-1 derepresses the cytoskeleton regulatory protein twinfilin-1 to provoke cardiac hypertrophy
    • Li Q, Song XW, Zou J, Wang GK, Kremneva E, Li XQ, Zhu N, Sun T, Lappalainen P, Yuan WJ, et al. 2010a. Attenuation of microRNA-1 derepresses the cytoskeleton regulatory protein twinfilin-1 to provoke cardiac hypertrophy. J Cell Sci 123: 2444-2452.
    • (2010) J Cell Sci , vol.123 , pp. 2444-2452
    • Li, Q.1    Song, X.W.2    Zou, J.3    Wang, G.K.4    Kremneva, E.5    Li, X.Q.6    Zhu, N.7    Sun, T.8    Lappalainen, P.9    Yuan, W.J.10
  • 118
    • 77954213976 scopus 로고    scopus 로고
    • Identification of glia maturation factor beta as an independent prognostic predictor for serous ovarian cancer
    • Li YL, Ye F, Cheng XD, Hu Y, Zhou CY, Lu WG, Xie X. 2010b. Identification of glia maturation factor beta as an independent prognostic predictor for serous ovarian cancer. Eur J Cancer 46: 2104-2118.
    • (2010) Eur J Cancer , vol.46 , pp. 2104-2118
    • Li, Y.L.1    Ye, F.2    Cheng, X.D.3    Hu, Y.4    Zhou, C.Y.5    Lu, W.G.6    Xie, X.7
  • 119
    • 0031027546 scopus 로고    scopus 로고
    • Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton
    • Lila T, Drubin DG. 1997. Evidence for physical and functional interactions among two Saccharomyces cerevisiae SH3 domain proteins, an adenylyl cyclase-associated protein and the actin cytoskeleton. Mol Biol Cell 8: 367-385.
    • (1997) Mol Biol Cell , vol.8 , pp. 367-385
    • Lila, T.1    Drubin, D.G.2
  • 120
    • 0024354003 scopus 로고
    • Purification and characterization of glia maturation factor beta: a growth regulator for neurons and glia
    • Lim R, Miller JF, Zaheer A. 1989. Purification and characterization of glia maturation factor beta: a growth regulator for neurons and glia. Proc Natl Acad Sci USA 86: 3901-3905.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3901-3905
    • Lim, R.1    Miller, J.F.2    Zaheer, A.3
  • 122
    • 77951197000 scopus 로고    scopus 로고
    • Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo
    • Lin MC, Galletta BJ, Sept D, Cooper JA. 2010. Overlapping and distinct functions for cofilin, coronin and Aip1 in actin dynamics in vivo. J Cell Sci 123: 1329-1342.
    • (2010) J Cell Sci , vol.123 , pp. 1329-1342
    • Lin, M.C.1    Galletta, B.J.2    Sept, D.3    Cooper, J.A.4
  • 123
    • 0031579458 scopus 로고    scopus 로고
    • Structure and expression of a novel filarial gene for glia maturation factor
    • Liu LX, Xu H, Weller PF, Shi A, Debnath I. 1997. Structure and expression of a novel filarial gene for glia maturation factor. Gene 186: 1-5.
    • (1997) Gene , vol.186 , pp. 1-5
    • Liu, L.X.1    Xu, H.2    Weller, P.F.3    Shi, A.4    Debnath, I.5
  • 124
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401: 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 125
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion
    • Maciver SK, Weeds AG. 1994. Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: consequences for cell locomotion. FEBS Lett 347: 251-256.
    • (1994) FEBS Lett , vol.347 , pp. 251-256
    • Maciver, S.K.1    Weeds, A.G.2
  • 126
    • 0021328060 scopus 로고
    • Isolation of low molecular weight actin-binding proteins from porcine brain
    • Maekawa S, Nishida E, Ohta Y, Sakai H. 1984. Isolation of low molecular weight actin-binding proteins from porcine brain. J Biochem 95: 377-385.
    • (1984) J Biochem , vol.95 , pp. 377-385
    • Maekawa, S.1    Nishida, E.2    Ohta, Y.3    Sakai, H.4
  • 127
    • 33847696641 scopus 로고    scopus 로고
    • Many faces of drebrin: from building dendritic spines and stabilizing gap junctions to shaping neurite-like cell processes
    • Majoul I, Shirao T, Sekino Y, Duden R. 2007. Many faces of drebrin: from building dendritic spines and stabilizing gap junctions to shaping neurite-like cell processes. Histochem Cell Biol 127: 355-361.
    • (2007) Histochem Cell Biol , vol.127 , pp. 355-361
    • Majoul, I.1    Shirao, T.2    Sekino, Y.3    Duden, R.4
  • 128
    • 6344225310 scopus 로고    scopus 로고
    • A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein
    • Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, Lappalainen P, Goode BL. 2004. A high-affinity interaction with ADP-actin monomers underlies the mechanism and in vivo function of Srv2/cyclase-associated protein. Mol Biol Cell 15: 5158-5171.
    • (2004) Mol Biol Cell , vol.15 , pp. 5158-5171
    • Mattila, P.K.1    Quintero-Monzon, O.2    Kugler, J.3    Moseley, J.B.4    Almo, S.C.5    Lappalainen, P.6    Goode, B.L.7
  • 129
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function
    • McGough A, Pope B, Chiu W, Weeds A. 1997. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol 138: 771-781.
    • (1997) J Cell Biol , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 130
    • 70349536006 scopus 로고    scopus 로고
    • In vivo RNAi screening identifies regulators of actin dynamics as key determinants of lymphoma progression
    • Meacham CE, Ho EE, Dubrovsky E, Gertler FB, Hemann MT. 2009. In vivo RNAi screening identifies regulators of actin dynamics as key determinants of lymphoma progression. Nat Genet 41: 1133-1137.
    • (2009) Nat Genet , vol.41 , pp. 1133-1137
    • Meacham, C.E.1    Ho, E.E.2    Dubrovsky, E.3    Gertler, F.B.4    Hemann, M.T.5
  • 133
    • 62649134712 scopus 로고    scopus 로고
    • Drebrin E is involved in the regulation of axonal growth through actin-myosin interactions
    • Mizui T, Kojima N, Yamazaki H, Katayama M, Hanamura K, Shirao T. 2009. Drebrin E is involved in the regulation of axonal growth through actin-myosin interactions. J Neurochem 109: 611-622.
    • (2009) J Neurochem , vol.109 , pp. 611-622
    • Mizui, T.1    Kojima, N.2    Yamazaki, H.3    Katayama, M.4    Hanamura, K.5    Shirao, T.6
  • 134
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon AL, Janmey PA, Louie KA, Drubin DG. 1993. Cofilin is an essential component of the yeast cortical cytoskeleton. J Cell Biol 120: 421-435.
    • (1993) J Cell Biol , vol.120 , pp. 421-435
    • Moon, A.L.1    Janmey, P.A.2    Louie, K.A.3    Drubin, D.G.4
  • 136
    • 0037093266 scopus 로고    scopus 로고
    • Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama K, Yahara I. 2002. Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J Cell Sci 115: 1591-601.
    • (2002) J Cell Sci , vol.115 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 137
    • 0026726153 scopus 로고
    • Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin
    • Moriyama K, Yonezawa N, Sakai H, Yahara I, Nishida E. 1992. Mutational analysis of an actin-binding site of cofilin and characterization of chimeric proteins between cofilin and destrin. J Biol Chem 267: 7240-7244.
    • (1992) J Biol Chem , vol.267 , pp. 7240-7244
    • Moriyama, K.1    Yonezawa, N.2    Sakai, H.3    Yahara, I.4    Nishida, E.5
  • 138
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama K, Iida K, Yahara I. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells 1: 73-86.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 139
    • 33646704772 scopus 로고    scopus 로고
    • Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo
    • Moseley JB, Okada K, Balcer HI, Kovar DR, Pollard TD, Goode BL. 2006. Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo. J Cell Sci 119: 1547-1557.
    • (2006) J Cell Sci , vol.119 , pp. 1547-1557
    • Moseley, J.B.1    Okada, K.2    Balcer, H.I.3    Kovar, D.R.4    Pollard, T.D.5    Goode, B.L.6
  • 141
    • 77953582940 scopus 로고    scopus 로고
    • GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton
    • Nakano K, Kuwayama H, Kawasaki M, Numata O, Takaine M. 2010. GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton. Cytoskeleton (Hoboken) 67: 373-382.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 373-382
    • Nakano, K.1    Kuwayama, H.2    Kawasaki, M.3    Numata, O.4    Takaine, M.5
  • 142
    • 0036202003 scopus 로고    scopus 로고
    • Cellular and humoral immune responses to a human pancreatic cancer antigen, coactosin-like protein, originally defined by the SEREX method
    • Nakatsura T, Senju S, Ito M, Nishimura Y, Itoh K. 2002. Cellular and humoral immune responses to a human pancreatic cancer antigen, coactosin-like protein, originally defined by the SEREX method. Eur J Immunol 32: 826-836.
    • (2002) Eur J Immunol , vol.32 , pp. 826-836
    • Nakatsura, T.1    Senju, S.2    Ito, M.3    Nishimura, Y.4    Itoh, K.5
  • 143
    • 58249091719 scopus 로고    scopus 로고
    • Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage
    • Nevalainen EM, Skwarek-Maruszewska A, Braun A, Moser M, Lappalainen P. 2009. Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage. Biochem J 417: 593-600.
    • (2009) Biochem J , vol.417 , pp. 593-600
    • Nevalainen, E.M.1    Skwarek-Maruszewska, A.2    Braun, A.3    Moser, M.4    Lappalainen, P.5
  • 144
    • 0021749110 scopus 로고
    • Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
    • Nishida E, Maekawa S, Sakai H. 1984. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry 23: 5307-5313.
    • (1984) Biochemistry , vol.23 , pp. 5307-5313
    • Nishida, E.1    Maekawa, S.2    Sakai, H.3
  • 145
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa R, Nagata-Ohashi K, Takeichi M, Mizuno K, Uemura T. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108: 233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 146
    • 0035951069 scopus 로고    scopus 로고
    • Identification of yeast cofilin residues specific for actin monomer and PIP2 binding
    • Ojala PJ, Paavilainen V, Lappalainen P. 2001. Identification of yeast cofilin residues specific for actin monomer and PIP2 binding. Biochemistry 40: 15562-15569.
    • (2001) Biochemistry , vol.40 , pp. 15562-15569
    • Ojala, P.J.1    Paavilainen, V.2    Lappalainen, P.3
  • 147
    • 0036854364 scopus 로고    scopus 로고
    • The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers
    • Ojala PJ, Paavilainen VO, Vartiainen MK, Tuma R, Weeds AG, Lappalainen P. 2002. The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers. Mol Biol Cell 13: 3811-3821.
    • (2002) Mol Biol Cell , vol.13 , pp. 3811-3821
    • Ojala, P.J.1    Paavilainen, V.O.2    Vartiainen, M.K.3    Tuma, R.4    Weeds, A.G.5    Lappalainen, P.6
  • 148
    • 0037044771 scopus 로고    scopus 로고
    • Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends
    • Okada K, Blanchoin L, Abe H, Chen H, Pollard TD, Bamburg JR. 2002. Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J Biol Chem 277: 43011-43016.
    • (2002) J Biol Chem , vol.277 , pp. 43011-43016
    • Okada, K.1    Blanchoin, L.2    Abe, H.3    Chen, H.4    Pollard, T.D.5    Bamburg, J.R.6
  • 149
    • 33745613278 scopus 로고    scopus 로고
    • Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments
    • Okada K, Ravi H, Smith EM, Goode BL. 2006. Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Mol Biol Cell 17: 2855-2868.
    • (2006) Mol Biol Cell , vol.17 , pp. 2855-2868
    • Okada, K.1    Ravi, H.2    Smith, E.M.3    Goode, B.L.4
  • 150
    • 34748872096 scopus 로고    scopus 로고
    • Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state
    • Okreglak V, Drubin DG. 2007. Cofilin recruitment and function during actin-mediated endocytosis dictated by actin nucleotide state. J Cell Biol 178: 1251-1264.
    • (2007) J Cell Biol , vol.178 , pp. 1251-1264
    • Okreglak, V.1    Drubin, D.G.2
  • 151
    • 77949679483 scopus 로고    scopus 로고
    • Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway
    • Okreglak V, Drubin DG. 2010. Loss of Aip1 reveals a role in maintaining the actin monomer pool and an in vivo oligomer assembly pathway. J Cell Biol 188: 769-777.
    • (2010) J Cell Biol , vol.188 , pp. 769-777
    • Okreglak, V.1    Drubin, D.G.2
  • 152
    • 45549095846 scopus 로고    scopus 로고
    • Actin-binding protein 1 regulates B cell receptor-mediated antigen processing and presentation in response to B cell receptor activation
    • Onabajo OO, Seeley MK, Kale A, Qualmann B, Kessels M, Han J, Tan TH, Song W. 2008. Actin-binding protein 1 regulates B cell receptor-mediated antigen processing and presentation in response to B cell receptor activation. J Immunol 180: 6685-6695.
    • (2008) J Immunol , vol.180 , pp. 6685-6695
    • Onabajo, O.O.1    Seeley, M.K.2    Kale, A.3    Qualmann, B.4    Kessels, M.5    Han, J.6    Tan, T.H.7    Song, W.8
  • 153
    • 0035911962 scopus 로고    scopus 로고
    • The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments
    • Ono S. 2001. The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments. J Cell Biol 152: 1313-1319.
    • (2001) J Cell Biol , vol.152 , pp. 1313-1319
    • Ono, S.1
  • 154
    • 0344391975 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filament
    • Ono, S. 2003. Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filament. Biochemistry 42: 13363-13370.
    • (2003) Biochemistry , vol.42 , pp. 13363-13370
    • Ono, S.1
  • 155
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono S, Ono K. 2002. Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J Cell Biol 156: 1065-1076.
    • (2002) J Cell Biol , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 156
    • 0035937148 scopus 로고    scopus 로고
    • 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
    • Ono S, McGough A, Pope BJ, Tolbert VT, Bui A, Pohl J, Benian GM, Gernert KM, Weeds AG. 2001. 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. J Biol Chem 276: 5952-5958.
    • (2001) J Biol Chem , vol.276 , pp. 5952-5958
    • Ono, S.1    McGough, A.2    Pope, B.J.3    Tolbert, V.T.4    Bui, A.5    Pohl, J.6    Benian, G.M.7    Gernert, K.M.8    Weeds, A.G.9
  • 157
    • 0037900004 scopus 로고    scopus 로고
    • Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans
    • Ono K, Parast M, Alberico C, Benian GM, Ono S. 2003. Specific requirement for two ADF/cofilin isoforms in distinct actin-dependent processes in Caenorhabditis elegans. J Cell Sci 116: 2073-2085.
    • (2003) J Cell Sci , vol.116 , pp. 2073-2085
    • Ono, K.1    Parast, M.2    Alberico, C.3    Benian, G.M.4    Ono, S.5
  • 158
    • 1842790731 scopus 로고    scopus 로고
    • Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin filaments
    • Ono S, Mohri K, Ono K. 2004. Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/Cofilin-bound actin filaments. J Biol Chem 279: 14207-14212.
    • (2004) J Biol Chem , vol.279 , pp. 14207-14212
    • Ono, S.1    Mohri, K.2    Ono, K.3
  • 159
    • 0037044818 scopus 로고    scopus 로고
    • Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin
    • Paavilainen VO, Merckel MC, Falck S, Ojala PJ, Pohl E, Wilmanns M, Lappalainen P. 2002. Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin. J Biol Chem 277: 43089-43095.
    • (2002) J Biol Chem , vol.277 , pp. 43089-43095
    • Paavilainen, V.O.1    Merckel, M.C.2    Falck, S.3    Ojala, P.J.4    Pohl, E.5    Wilmanns, M.6    Lappalainen, P.7
  • 162
    • 47549090623 scopus 로고    scopus 로고
    • Structure of the actin-depolymerizing factor homology domain in complex with actin
    • Paavilainen VO, Oksanen E, Goldman A, Lappalainen P. 2008. Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol 182: 51-59.
    • (2008) J Cell Biol , vol.182 , pp. 51-59
    • Paavilainen, V.O.1    Oksanen, E.2    Goldman, A.3    Lappalainen, P.4
  • 163
    • 0035886026 scopus 로고    scopus 로고
    • Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
    • Palmgren S, Ojala PJ, Wear MA, Cooper JA, Lappalainen P. 2001. Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J Cell Biol 155: 251-260.
    • (2001) J Cell Biol , vol.155 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 164
    • 0034810288 scopus 로고    scopus 로고
    • Drebrin particles: components in the ensemble of proteins regulating actin dynamics of lamellipodia and filopodia
    • Peitsch WK, Hofmann I, Pratzel S, Grund C, Kuhn C, Moll I, Langbein L, Franke WW. 2001. Drebrin particles: components in the ensemble of proteins regulating actin dynamics of lamellipodia and filopodia. Eur J Cell Biol 80: 567-579.
    • (2001) Eur J Cell Biol , vol.80 , pp. 567-579
    • Peitsch, W.K.1    Hofmann, I.2    Pratzel, S.3    Grund, C.4    Kuhn, C.5    Moll, I.6    Langbein, L.7    Franke, W.W.8
  • 165
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans L, Fava E, Grabner H, Hannus M, Habermann B, Krausz E, Zerial M. 2005. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 436: 78-86.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6    Zerial, M.7
  • 166
  • 167
    • 77952123773 scopus 로고    scopus 로고
    • Actin filament remodeling by actin depolymerization factor/cofilin
    • Pfaendtner J, De La Cruz EM, Voth GA. 2010. Actin filament remodeling by actin depolymerization factor/cofilin. Proc Natl Acad Sci USA 107: 7299-7304.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7299-7304
    • Pfaendtner, J.1    De La Cruz, E.M.2    Voth, G.A.3
  • 168
    • 35348895757 scopus 로고    scopus 로고
    • Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal morphology
    • Pinyol R, Haeckel A, Ritter A, Qualmann B, Kessels MM. 2007. Regulation of N-WASP and the Arp2/3 complex by Abp1 controls neuronal morphology. PLoS One 2: e400.
    • (2007) PLoS One , vol.2
    • Pinyol, R.1    Haeckel, A.2    Ritter, A.3    Qualmann, B.4    Kessels, M.M.5
  • 169
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard TD, Cooper JA. 2009. Actin, a central player in cell shape and movement. Science 326: 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 171
    • 0035886877 scopus 로고    scopus 로고
    • Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75
    • Provost P, Doucet J, Stock A, Gerisch G, Samuelsson B, Radmark O. 2001b. Coactosin-like protein, a human F-actin-binding protein: critical role of lysine-75. Biochem J 359: 255-263.
    • (2001) Biochem J , vol.359 , pp. 255-263
    • Provost, P.1    Doucet, J.2    Stock, A.3    Gerisch, G.4    Samuelsson, B.5    Radmark, O.6
  • 172
    • 1542620777 scopus 로고    scopus 로고
    • Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family
    • Qualmann B, Boeckers TM, Jeromin M, Gundelfinger ED, Kessels MM. 2004. Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family. J Neurosci 24: 2481-2495.
    • (2004) J Neurosci , vol.24 , pp. 2481-2495
    • Qualmann, B.1    Boeckers, T.M.2    Jeromin, M.3    Gundelfinger, E.D.4    Kessels, M.M.5
  • 173
    • 21844474822 scopus 로고    scopus 로고
    • Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions
    • Quintero-Monzon O, Rodal AA, Strokopytov B, Almo SC, Goode BL. 2005. Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions. Mol Biol Cell 16: 3128-3139.
    • (2005) Mol Biol Cell , vol.16 , pp. 3128-3139
    • Quintero-Monzon, O.1    Rodal, A.A.2    Strokopytov, B.3    Almo, S.C.4    Goode, B.L.5
  • 174
    • 67449107876 scopus 로고    scopus 로고
    • Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover
    • Quintero-Monzon O, Jonasson EM, Bertling E, Talarico L, Chaudhry F, Sihvo M, Lappalainen P, Goode BL. 2009. Reconstitution and dissection of the 600-kDa Srv2/CAP complex: roles for oligomerization and cofilin-actin binding in driving actin turnover. J Biol Chem 284: 10923-10934.
    • (2009) J Biol Chem , vol.284 , pp. 10923-10934
    • Quintero-Monzon, O.1    Jonasson, E.M.2    Bertling, E.3    Talarico, L.4    Chaudhry, F.5    Sihvo, M.6    Lappalainen, P.7    Goode, B.L.8
  • 175
    • 34548409590 scopus 로고    scopus 로고
    • The flare gene, which encodes the AIP1 protein of Drosophila, functions to regulate F-actin disassembly in pupal epidermal cells
    • Ren N, Charlton J, Adler PN. 2007. The flare gene, which encodes the AIP1 protein of Drosophila, functions to regulate F-actin disassembly in pupal epidermal cells. Genetics 176: 2223-2234.
    • (2007) Genetics , vol.176 , pp. 2223-2234
    • Ren, N.1    Charlton, J.2    Adler, P.N.3
  • 176
    • 0032516848 scopus 로고    scopus 로고
    • 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
    • Ressad F, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D, Carlier MF. 1998. 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. J Biol Chem 273: 20894-20902.
    • (1998) J Biol Chem , vol.273 , pp. 20894-20902
    • Ressad, F.1    Didry, D.2    Xia, G.X.3    Hong, Y.4    Chua, N.H.5    Pantaloni, D.6    Carlier, M.F.7
  • 179
    • 70349622812 scopus 로고    scopus 로고
    • MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear
    • Rzadzinska AK, Nevalainen EM, Prosser HM, Lappalainen P, Steel KP. 2009. MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear. PLoS One 4: e7097.
    • (2009) PLoS One , vol.4
    • Rzadzinska, A.K.1    Nevalainen, E.M.2    Prosser, H.M.3    Lappalainen, P.4    Steel, K.P.5
  • 180
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas J, Zhao H, Lappalainen P. 2010. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol Rev 90: 259-289.
    • (2010) Physiol Rev , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 181
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y, Hayashi K, Shirao T, Ishikawa R, Kohama K. 1996. Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J Neurochem 66: 980-988.
    • (1996) J Neurochem , vol.66 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 182
    • 79851502285 scopus 로고    scopus 로고
    • Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution
    • Sharma S, Grintsevich EE, Phillips ML, Reisler E, Gimzewski JK. 2011. Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution. Nano Lett 11: 825-827.
    • (2011) Nano Lett , vol.11 , pp. 825-827
    • Sharma, S.1    Grintsevich, E.E.2    Phillips, M.L.3    Reisler, E.4    Gimzewski, J.K.5
  • 183
    • 24344440631 scopus 로고    scopus 로고
    • A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers
    • Schüler H, Mueller AK, Matuschewski K. 2005. A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers. Mol Biol Cell 16: 4013-4023.
    • (2005) Mol Biol Cell , vol.16 , pp. 4013-4023
    • Schüler, H.1    Mueller, A.K.2    Matuschewski, K.3
  • 185
    • 79953161643 scopus 로고    scopus 로고
    • The mammalian actin-binding protein 1 (mAbp1): a novel molecular player in leukocyte biology
    • Schymeinsky J, Sperandio M, Walzog B. 2011. The mammalian actin-binding protein 1 (mAbp1): a novel molecular player in leukocyte biology. Trends Cell Bio l21: 247-255.
    • (2011) Trends Cell Bio , vol.121 , pp. 247-255
    • Schymeinsky, J.1    Sperandio, M.2    Walzog, B.3
  • 186
    • 77951757643 scopus 로고    scopus 로고
    • Pseudopodial actin dynamics control epithelial-mesenchymal transition in metastatic cancer cells
    • Shankar J, Messenberg A, Chan J, Underhill TM, Foster LJ, Nabi IR. 2010. Pseudopodial actin dynamics control epithelial-mesenchymal transition in metastatic cancer cells. Cancer Res 70: 3780-3790.
    • (2010) Cancer Res , vol.70 , pp. 3780-3790
    • Shankar, J.1    Messenberg, A.2    Chan, J.3    Underhill, T.M.4    Foster, L.J.5    Nabi, I.R.6
  • 187
    • 0037166050 scopus 로고    scopus 로고
    • Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome
    • Shim KS, Lubec G. 2002. Drebrin, a dendritic spine protein, is manifold decreased in brains of patients with Alzheimer's disease and Down syndrome. Neurosci Lett 324: 209-212.
    • (2002) Neurosci Lett , vol.324 , pp. 209-212
    • Shim, K.S.1    Lubec, G.2
  • 189
    • 0023793340 scopus 로고
    • Molecular cloning of a cDNA for the developmentally regulated brain protein, drebrin
    • Shirao T, Kojima N, Kato Y, Obata K. 1988. Molecular cloning of a cDNA for the developmentally regulated brain protein, drebrin. Brain Res 464: 71-74.
    • (1988) Brain Res , vol.464 , pp. 71-74
    • Shirao, T.1    Kojima, N.2    Kato, Y.3    Obata, K.4
  • 190
    • 77955647583 scopus 로고    scopus 로고
    • Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast
    • Sirotkin V, Berro J, Macmillan K, Zhao L, Pollard TD. 2010. Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast. Mol Biol Cell 21: 2894-2904.
    • (2010) Mol Biol Cell , vol.21 , pp. 2894-2904
    • Sirotkin, V.1    Berro, J.2    Macmillan, K.3    Zhao, L.4    Pollard, T.D.5
  • 191
    • 77957850795 scopus 로고    scopus 로고
    • Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast
    • Skau CT, Kovar DR. 2010. Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast. Curr Biol 20: 1415-1422.
    • (2010) Curr Biol , vol.20 , pp. 1415-1422
    • Skau, C.T.1    Kovar, D.R.2
  • 192
    • 33746861083 scopus 로고    scopus 로고
    • Initiation of cofilin activity in response to EGF is uncoupled from cofilin phosphorylation and dephosphorylation in carcinoma cells
    • Song X, Chen X, Yamaguchi H, Mouneimne G, Condeelis JS, Eddy RJ. 2006. Initiation of cofilin activity in response to EGF is uncoupled from cofilin phosphorylation and dephosphorylation in carcinoma cells. J Cell Sci 119: 2871-2881.
    • (2006) J Cell Sci , vol.119 , pp. 2871-2881
    • Song, X.1    Chen, X.2    Yamaguchi, H.3    Mouneimne, G.4    Condeelis, J.S.5    Eddy, R.J.6
  • 194
    • 24044475924 scopus 로고    scopus 로고
    • Phased translation function revisited: structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches
    • Strokopytov BV, Fedorov A, Mahoney NM, Kessels M, Drubin DG, Almo SC. 2005. Phased translation function revisited: structure solution of the cofilin-homology domain from yeast actin-binding protein 1 using six-dimensional searches. Acta Crystallogr D Biol Crystallogr. 61: 285-293.
    • (2005) Acta Crystallogr D Biol Crystallogr. , vol.61 , pp. 285-293
    • Strokopytov, B.V.1    Fedorov, A.2    Mahoney, N.M.3    Kessels, M.4    Drubin, D.G.5    Almo, S.C.6
  • 196
    • 33745535568 scopus 로고    scopus 로고
    • Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity
    • Sun Y, Martin AC, Drubin DG. 2006. Endocytic internalization in budding yeast requires coordinated actin nucleation and myosin motor activity. Dev Cell 11: 33-46.
    • (2006) Dev Cell , vol.11 , pp. 33-46
    • Sun, Y.1    Martin, A.C.2    Drubin, D.G.3
  • 197
    • 0037081289 scopus 로고    scopus 로고
    • Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene
    • Takahashi H, Koshimizu U, Miyazaki J, Nakamura T. 2002. Impaired spermatogenic ability of testicular germ cells in mice deficient in the LIM-kinase 2 gene. Dev Biol 241: 259-272.
    • (2002) Dev Biol , vol.241 , pp. 259-272
    • Takahashi, H.1    Koshimizu, U.2    Miyazaki, J.3    Nakamura, T.4
  • 198
    • 0041342023 scopus 로고    scopus 로고
    • Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis
    • Takahashi H, Sekino Y, Tanaka S, Mizui T, Kishi S, Shirao T. 2003. Drebrin-dependent actin clustering in dendritic filopodia governs synaptic targeting of postsynaptic density-95 and dendritic spine morphogenesis. J Neurosci 23: 6586-6595.
    • (2003) J Neurosci , vol.23 , pp. 6586-6595
    • Takahashi, H.1    Sekino, Y.2    Tanaka, S.3    Mizui, T.4    Kishi, S.5    Shirao, T.6
  • 199
    • 33646830444 scopus 로고    scopus 로고
    • Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones
    • Takahashi H, Mizui T, Shirao T. 2006. Down-regulation of drebrin A expression suppresses synaptic targeting of NMDA receptors in developing hippocampal neurones. J Neurochem 97: Suppl 1 110-115.
    • (2006) J Neurochem , vol.97 , Issue.SUPPL. 1 , pp. 110-115
    • Takahashi, H.1    Mizui, T.2    Shirao, T.3
  • 200
    • 48049092280 scopus 로고    scopus 로고
    • Focused microarray analysis of peripheral mononuclear blood cells from Churg-Strauss syndrome patients
    • Tougan T, Onda H, Okuzaki D, Kobayashi S, Hashimoto H, Nojima H. 2008. Focused microarray analysis of peripheral mononuclear blood cells from Churg-Strauss syndrome patients. DNA Res 15: 103-114.
    • (2008) DNA Res , vol.15 , pp. 103-114
    • Tougan, T.1    Onda, H.2    Okuzaki, D.3    Kobayashi, S.4    Hashimoto, H.5    Nojima, H.6
  • 202
    • 70349125020 scopus 로고    scopus 로고
    • Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets
    • Tucker KL, Kaiser WJ, Bergeron AL, Hu H, Dong JF, Tan TH, Gibbins JM. 2009. Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets. Proteomics 9: 4340-4354.
    • (2009) Proteomics , vol.9 , pp. 4340-4354
    • Tucker, K.L.1    Kaiser, W.J.2    Bergeron, A.L.3    Hu, H.4    Dong, J.F.5    Tan, T.H.6    Gibbins, J.M.7
  • 203
    • 33746375657 scopus 로고    scopus 로고
    • Coronins: the return of the crown
    • Uetrecht AC, Bear JE. 2006. Coronins: the return of the crown. Trends Cell Biol 16: 421-426.
    • (2006) Trends Cell Biol , vol.16 , pp. 421-426
    • Uetrecht, A.C.1    Bear, J.E.2
  • 205
    • 0034633937 scopus 로고    scopus 로고
    • The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant
    • Van Troys M, Dewitte D, Verschelde JL, Goethals M, Vandekerckhove J, Ampe C. 2000. The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant. Biochemistry 39: 12181-12189.
    • (2000) Biochemistry , vol.39 , pp. 12181-12189
    • Van Troys, M.1    Dewitte, D.2    Verschelde, J.L.3    Goethals, M.4    Vandekerckhove, J.5    Ampe, C.6
  • 207
    • 0033976663 scopus 로고    scopus 로고
    • Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics
    • Vartiainen M, Ojala PJ, Auvinen P, Peranen J, Lappalainen P. 2000. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol Cell Biol 20: 1772-1783.
    • (2000) Mol Cell Biol , vol.20 , pp. 1772-1783
    • Vartiainen, M.1    Ojala, P.J.2    Auvinen, P.3    Peranen, J.4    Lappalainen, P.5
  • 208
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • Vartiainen MK, Mustonen T, Mattila PK, Ojala PJ, Thesleff I, Partanen J, Lappalainen P. 2002. The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics. Mol Biol Cell 13: 183-194.
    • (2002) Mol Biol Cell , vol.13 , pp. 183-194
    • Vartiainen, M.K.1    Mustonen, T.2    Mattila, P.K.3    Ojala, P.J.4    Thesleff, I.5    Partanen, J.6    Lappalainen, P.7
  • 209
    • 0141445987 scopus 로고    scopus 로고
    • Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated
    • Vartiainen MK, Sarkkinen EM, Matilainen T, Salminen M, Lappalainen P. 2003. Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated. J Biol Chem 278: 34347-34355.
    • (2003) J Biol Chem , vol.278 , pp. 34347-34355
    • Vartiainen, M.K.1    Sarkkinen, E.M.2    Matilainen, T.3    Salminen, M.4    Lappalainen, P.5
  • 211
    • 16844372470 scopus 로고    scopus 로고
    • Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin
    • Wang Y, Shibasaki F, Mizuno K. 2005. Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin. J Biol Chem 280: 12683-12689.
    • (2005) J Biol Chem , vol.280 , pp. 12683-12689
    • Wang, Y.1    Shibasaki, F.2    Mizuno, K.3
  • 212
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • Wang W, Eddy R, Condeelis J. 2007. The cofilin pathway in breast cancer invasion and metastasis. Nat Rev Cancer 7: 429-440.
    • (2007) Nat Rev Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 214
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: new insights into mechanism and regulation
    • Wear MA, Cooper JA. 2004. Capping protein: new insights into mechanism and regulation. Trends Biochem Sci 29: 418-428.
    • (2004) Trends Biochem Sci , vol.29 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 218
    • 27444441098 scopus 로고    scopus 로고
    • The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization
    • Yamashiro S, Mohri K, Ono S. 2005. The two Caenorhabditis elegans actin-depolymerizing factor/cofilin proteins differently enhance actin filament severing and depolymerization. Biochemistry 44: 14238-14247.
    • (2005) Biochemistry , vol.44 , pp. 14238-14247
    • Yamashiro, S.1    Mohri, K.2    Ono, S.3
  • 219
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • Yeoh S, Pope B, Mannherz HG, Weeds A. 2002. Determining the differences in actin binding by human ADF and cofilin. J Mol Biol 315: 911-925.
    • (2002) J Mol Biol , vol.315 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 220
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H. 1990. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 265: 8382-8386.
    • (1990) J Biol Chem , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 221
    • 74449092215 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway
    • Yoo Y, Ho HJ, Wang C, Guan JL. 2010. Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway. Oncogene 29: 263-272.
    • (2010) Oncogene , vol.29 , pp. 263-272
    • Yoo, Y.1    Ho, H.J.2    Wang, C.3    Guan, J.L.4
  • 222
    • 0027403057 scopus 로고
    • Expression of glia maturation factor beta mRNA and protein in rat organs and cells
    • Zaheer A, Fink BD, Lim R. 1993. Expression of glia maturation factor beta mRNA and protein in rat organs and cells. J Neurochem 60: 914-920.
    • (1993) J Neurochem , vol.60 , pp. 914-920
    • Zaheer, A.1    Fink, B.D.2    Lim, R.3
  • 223
    • 33745045434 scopus 로고    scopus 로고
    • GMF-knockout mice are unable to induce brain-derived neurotrophic factor after exercise
    • Zaheer A, Haas JT, Reyes C, Mathur SN, Yang B, Lim R. 2006. GMF-knockout mice are unable to induce brain-derived neurotrophic factor after exercise. Neurochem Res 31: 579-584.
    • (2006) Neurochem Res , vol.31 , pp. 579-584
    • Zaheer, A.1    Haas, J.T.2    Reyes, C.3    Mathur, S.N.4    Yang, B.5    Lim, R.6
  • 224
    • 33845871981 scopus 로고    scopus 로고
    • Reduced severity of experimental autoimmune encephalomyelitis in GMF-deficient mice
    • Zaheer A, Zaheer S, Sahu SK, Yang B, Lim R. 2007. Reduced severity of experimental autoimmune encephalomyelitis in GMF-deficient mice. Neurochem Res 32: 39-47.
    • (2007) Neurochem Res , vol.32 , pp. 39-47
    • Zaheer, A.1    Zaheer, S.2    Sahu, S.K.3    Yang, B.4    Lim, R.5
  • 226
    • 77956646000 scopus 로고    scopus 로고
    • ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor
    • Zhao H, Hakala M, Lappalainen P. 2010. ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor. Biophys J 98: 2327-2336.
    • (2010) Biophys J , vol.98 , pp. 2327-2336
    • Zhao, H.1    Hakala, M.2    Lappalainen, P.3


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