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Volumn 43, Issue 22, 2004, Pages 7127-7142

In vitro activity differences between proteins of the ADF/cofilin family define two distinct subgroups

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CELLS; DEPOLYMERIZATION; PH EFFECTS; YEAST;

EID: 2642580847     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049797n     Document Type: Article
Times cited : (70)

References (104)
  • 1
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/Cofilin family: Essential regulators of actin dynamics
    • Bamburg, J. R. (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
  • 2
    • 0023571668 scopus 로고
    • Distribution and cellular localization of actin depolymerizing factor
    • Bamburg, J. R., and Bray, D. (1987) Distribution and cellular localization of actin depolymerizing factor, J. Cell Biol. 105, 2817-2825.
    • (1987) J. Cell Biol. , vol.105 , pp. 2817-2825
    • Bamburg, J.R.1    Bray, D.2
  • 3
    • 0023428481 scopus 로고
    • Distribution among tissues and intracellular localization of cofilin, a 21kDa actin-binding protein
    • Yonezawa, N., Nishida, E., Koyasu, S., Maekawa, S., Ohta, Y., Yahara, I., and Sakai, H. (1987) Distribution among tissues and intracellular localization of cofilin, a 21kDa actin-binding protein, Cell Struct. Funct. 12, 443-452.
    • (1987) Cell Struct. Funct. , vol.12 , pp. 443-452
    • Yonezawa, N.1    Nishida, E.2    Koyasu, S.3    Maekawa, S.4    Ohta, Y.5    Yahara, I.6    Sakai, H.7
  • 4
    • 0027446345 scopus 로고
    • Cofilin is an essential component of the yeast cortical cytoskeleton
    • Moon, A. L., Janmey, P. A., Louie, K. A., and Drubin, D. G. (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
  • 5
    • 0028955146 scopus 로고
    • Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action
    • Nagaoka, R., Kusano, K., Abe, H., and Obinata, T. (1995) Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action, J. Cell Sci. 108, 581-593.
    • (1995) J. Cell Sci. , vol.108 , pp. 581-593
    • Nagaoka, R.1    Kusano, K.2    Abe, H.3    Obinata, T.4
  • 6
    • 0028799957 scopus 로고
    • Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue, result in defects in centrosome migration and cytokinesis
    • Gunsalus, K. C., Bonaccorsi, S., Williams, E., Verni, F., Gatti, M., and Goldberg, M. L. (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
  • 7
    • 0029867539 scopus 로고    scopus 로고
    • Xenopus laevis actin-depolymerizing factor/cofilin: A phosphorylation-regulated protein essential for development
    • Abe, H., Obinata, T., Minamide, L. S., and Bamburg, J. R. (1996) Xenopus laevis actin-depolymerizing factor/cofilin: a phosphorylation-regulated protein essential for development, J. Cell Biol. 132, 871-885.
    • (1996) J. Cell Biol. , vol.132 , pp. 871-885
    • Abe, H.1    Obinata, T.2    Minamide, L.S.3    Bamburg, J.R.4
  • 8
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen, P., and Drubin, D. G. (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
  • 9
    • 0030821155 scopus 로고    scopus 로고
    • Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • Rosenblatt, J., Agnew, B. J., Abe, H., Bamburg, J. R., and Mitchison, T. J. (1997) Xenopus actin depolymerizing factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails, J. Cell Biol. 136, 1323-1332.
    • (1997) J. Cell Biol. , vol.136 , pp. 1323-1332
    • Rosenblatt, J.1    Agnew, B.J.2    Abe, H.3    Bamburg, J.R.4    Mitchison, T.J.5
  • 10
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M. F., Laurent, V., Santolini, J., Melki, R., Didry, D., Xia, G. X., Hong, Y., Chua, N. H., and Pantaloni, D. (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility, J. Cell Biol. 136, 1307-1322.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 11
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel, T. P., Boujemaa, R., Pantaloni, D., and Carlier, M. F. (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
  • 12
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis, J. S. (2001) How is actin polymerization nucleated in vivo? Trends Cell Biol. 11, 288-293.
    • (2001) Trends Cell Biol. , vol.11 , pp. 288-293
    • Condeelis, J.S.1
  • 13
    • 12244303674 scopus 로고    scopus 로고
    • ADF/cofilin controls cell polarity during fibroblast migration
    • Dawe, H. R., Minamide, L. S., Bamburg, J. R., and Cramer, L. P. (2003) ADF/cofilin controls cell polarity during fibroblast migration, Curr. Biol. 13, 252-257.
    • (2003) Curr. Biol. , vol.13 , pp. 252-257
    • Dawe, H.R.1    Minamide, L.S.2    Bamburg, J.R.3    Cramer, L.P.4
  • 14
    • 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., and 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
  • 15
    • 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, V. E., Orlova, A., Lukoyanova, N., Wriggers, W., and Egelman, E. H. (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
  • 16
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden, S. M., Miller, P. S., Brauweiler, A., and Bamburg, J. R. (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
  • 17
    • 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., and 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
  • 18
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M., Pope, B., Maciver, S. K., and Weeds, A. G. (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
  • 19
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin, L., and Pollard, T. D. (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
  • 20
    • 0032516848 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of acfin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation
    • Ressad, F., Didry, D., Xia, G. X., Hong, Y., Chua, N. H., Pantaloni, D., and Carlier, M. F. (1998) Kinetic analysis of the interaction of acfin-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
  • 21
    • 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., and 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
  • 22
    • 0020025754 scopus 로고
    • Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF)
    • Bernstein, B. W., and Bamburg, J. R. (1982) Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF), Cell Motil. 2, 1-8.
    • (1982) Cell Motil. , vol.2 , pp. 1-8
    • Bernstein, B.W.1    Bamburg, J.R.2
  • 23
    • 0022410877 scopus 로고
    • An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin
    • Nishida, E., Muneyuki, E., Maekawa, S., Ohta, Y., and Sakai, H. (1985) An actin-depolymerizing protein (destrin) from porcine kidney. Its action on F-actin containing or lacking tropomyosin, Biochemistry 24, 6624-6630.
    • (1985) Biochemistry , vol.24 , pp. 6624-6630
    • Nishida, E.1    Muneyuki, E.2    Maekawa, S.3    Ohta, Y.4    Sakai, H.5
  • 25
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B. J., Minamide, L. S., and Bamburg, J. R. (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
  • 26
    • 0032053115 scopus 로고    scopus 로고
    • Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity
    • Smertenko, A. P., Jiang, C. J., Simmons, N. J., Weeds, A. G., Davies, D. R., and Hussey, P. J. (1998) Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity, Plant J. 14, 187-193.
    • (1998) Plant J. , vol.14 , pp. 187-193
    • Smertenko, A.P.1    Jiang, C.J.2    Simmons, N.J.3    Weeds, A.G.4    Davies, D.R.5    Hussey, P.J.6
  • 27
    • 0034645797 scopus 로고    scopus 로고
    • Phosphorylation of Acanthamoeba actophorin (ADF/cofilin) blocks interaction with actin without a change in atomic structure
    • Blanchoin, L., Robinson, R. C., Choe, S., and Pollard, T. D. (2000) 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
  • 29
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K., Nagata, K., Wada, A., Kangawa, K., Nishida, E., and Mizuno, K. (1998) Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization, Nature 393, 809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8
  • 30
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphoylation and actin cytoskeletal dynamics regulated by Rho- and Cdc42-actiated LIM-kinase 2
    • Sumi, T., Matsumoto, K., Takai, Y., and Nakamura, T. (1999) Cofilin phosphoylation and actin cytoskeletal dynamics regulated by Rho- and Cdc42-actiated LIM-kinase 2, J. Cell Biol. 147, 1519-1532.
    • (1999) J. Cell Biol. , vol.147 , pp. 1519-1532
    • Sumi, T.1    Matsumoto, K.2    Takai, Y.3    Nakamura, T.4
  • 32
    • 0035865682 scopus 로고    scopus 로고
    • LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505
    • Amano, T., Tanabe, K., Eto, T., Narumiya, S., and Mizuno, K. (2001) LIM-kinase 2 induces formation of stress fibres, focal adhesions and membrane blebs, dependent on its activation by Rho-associated kinase-catalysed phosphorylation at threonine-505, Biochem. J. 354, 149-159.
    • (2001) Biochem. J. , vol.354 , pp. 149-159
    • Amano, T.1    Tanabe, K.2    Eto, T.3    Narumiya, S.4    Mizuno, K.5
  • 33
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima, J., Toshima, J. Y., Amano, T., Yang, N., Narumiya, S., and Mizuno, K. (2001) Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation, Mol. Biol. Cell 12, 1131-1145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 34
    • 0035903099 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells
    • Toshima, J., Toshima, J. Y., Takeuchi, K., Mori, R., and Mizuno, K. (2001) Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells, J. Biol. Chem. 276, 31449-31458.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31449-31458
    • Toshima, J.1    Toshima, J.Y.2    Takeuchi, K.3    Mori, R.4    Mizuno, K.5
  • 35
    • 0035171699 scopus 로고    scopus 로고
    • Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation
    • Toshima, J., Toshima, J. Y., Amano, T., Yang, N., Narumiya, S., and Mizuno, K. (2001) Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation, Mol. Biol. Cell 12, 1131-1145.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1131-1145
    • Toshima, J.1    Toshima, J.Y.2    Amano, T.3    Yang, N.4    Narumiya, S.5    Mizuno, K.6
  • 36
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • Gohla, A., and Bokoch, G. M. (2002) 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin, Curr. Biol. 12, 1704-1710.
    • (2002) Curr. Biol. , vol.12 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 37
    • 0037270323 scopus 로고    scopus 로고
    • Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta
    • Birkenfeld, J., Betz, H., and Roth, D. (2003) Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta, Biochem. J. 369, 45-54.
    • (2003) Biochem. J. , vol.369 , pp. 45-54
    • Birkenfeld, J.1    Betz, H.2    Roth, D.3
  • 38
    • 0035900680 scopus 로고    scopus 로고
    • Binding of 14-3-3beta regulates the kinase activity and subcellular localization of testicular protein kinase 1
    • Toshima, J. Y., Toshima, J., Watanabe, T., and Mizuno, K. (2001) Binding of 14-3-3beta regulates the kinase activity and subcellular localization of testicular protein kinase 1, J. Biol. Chem. 276, 43471-43481.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43471-43481
    • Toshima, J.Y.1    Toshima, J.2    Watanabe, T.3    Mizuno, K.4
  • 39
    • 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., and 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
  • 40
    • 0142155224 scopus 로고    scopus 로고
    • Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin
    • Ohta, Y., Kousaka, K., Nagata-Ohashi, K., Ohashi, K., Muramoto, A., Shima, Y., Niwa, R., Uemura, T., and Mizuno, K. (2003) Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin, Genes Cells 8, 811-824.
    • (2003) Genes Cells , vol.8 , pp. 811-824
    • Ohta, Y.1    Kousaka, K.2    Nagata-Ohashi, K.3    Ohashi, K.4    Muramoto, A.5    Shima, Y.6    Niwa, R.7    Uemura, T.8    Mizuno, K.9
  • 41
    • 0036900955 scopus 로고    scopus 로고
    • ADF/cofilin and actin dynamics in disease
    • Bamburg, J. R., and Wiggan, O. P. (2002) ADF/cofilin and actin dynamics in disease, Trends Cell Biol. 12, 598-605.
    • (2002) Trends Cell Biol. , vol.12 , pp. 598-605
    • Bamburg, J.R.1    Wiggan, O.P.2
  • 42
    • 15144352303 scopus 로고    scopus 로고
    • 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
    • Maciver, S. K., Pope, B. J., Whytock, S., and Weeds, A. G. (1998) 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, Eur. J. Biochem. 256, 388-397.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 388-397
    • Maciver, S.K.1    Pope, B.J.2    Whytock, S.3    Weeds, A.G.4
  • 44
    • 0031878090 scopus 로고    scopus 로고
    • The ADF homology (ADF-H) domain: A highly exploited actin-binding module
    • Lappalainen, P., Kessels, M. M., Cope, M. J., and Drubin, D. G. (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
  • 45
    • 0027475652 scopus 로고
    • Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein
    • Iida, K., Moriyama, K., Matsumoto, S., Kawasaki, H., Nishida, E., and Yahara, I. (1993) Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein, Gene 124, 115-120.
    • (1993) Gene , vol.124 , pp. 115-120
    • Iida, K.1    Moriyama, K.2    Matsumoto, S.3    Kawasaki, H.4    Nishida, E.5    Yahara, I.6
  • 46
    • 0032488999 scopus 로고    scopus 로고
    • Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics
    • Ono, S., and Benian, G. M. (1998) Two Caenorhabditis elegans actin depolymerizing factor/cofilin proteins, encoded by the unc-60 gene, differentially regulate actin filament dynamics, J. Biol. Chem. 273, 3778-3783.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3778-3783
    • Ono, S.1    Benian, G.M.2
  • 47
    • 0036153765 scopus 로고    scopus 로고
    • The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics
    • Vartiainen, M. K., Mustonen, T., Mattila, P. K., Ojala, P. J., Thesleff, I., Partanen, J., and 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
  • 48
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • Yeoh, S., Pope, B., Mannherz, H. G., and 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
  • 49
    • 1842829164 scopus 로고    scopus 로고
    • Efficient Salmonella entry requires activity cycles of host ADF and cofilin
    • Dai, S., Sarmiere, P. D., Wiggan, O., Bamburg, J. R., and Zhou, D. (2004) Efficient Salmonella entry requires activity cycles of host ADF and cofilin, Cell Microbiol. 6, 459-471.
    • (2004) Cell Microbiol. , vol.6 , pp. 459-471
    • Dai, S.1    Sarmiere, P.D.2    Wiggan, O.3    Bamburg, J.R.4    Zhou, D.5
  • 50
    • 0020021878 scopus 로고
    • Purification of muscle actin
    • Pardee, J. D., and Spudich, J. A. (1982) Purification of muscle actin, Methods Enzymol. 85 Pt. B, 164-181.
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 164-181
    • Pardee, J.D.1    Spudich, J.A.2
  • 51
    • 0027418763 scopus 로고
    • Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates
    • Kinosian, H. J., Selden, L. A., Estes, J. E., and Gershman, L. C. (1993) Nucleotide binding to actin. Cation dependence of nucleotide dissociation and exchange rates, J. Biol. Chem. 268, 8683-8691.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8683-8691
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 54
    • 0025050666 scopus 로고
    • Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor
    • Adams, M. E., Minamide, L. S., Duester, G., and Bamburg, J. R. (1990) Nucleotide sequence and expression of a cDNA encoding chick brain actin depolymerizing factor, Biochemistry 29, 7414-7420.
    • (1990) Biochemistry , vol.29 , pp. 7414-7420
    • Adams, M.E.1    Minamide, L.S.2    Duester, G.3    Bamburg, J.R.4
  • 55
    • 0024468554 scopus 로고
    • A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle
    • Abe, H., Ohshima, S., and Obinata, T. (1989) A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle, J. Biochem. 106, 696-702.
    • (1989) J. Biochem. , vol.106 , pp. 696-702
    • Abe, H.1    Ohshima, S.2    Obinata, T.3
  • 56
    • 0029904960 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the phosphorylation site of cofilin: Its role in cofilin-actin interaction and cytoplasmic localization
    • Nagaoka, R., Abe, H., and Obinata, T. (1996) Site-directed mutagenesis of the phosphorylation site of cofilin: its role in cofilin-actin interaction and cytoplasmic localization, Cell Motil. Cytoskeleton 35, 200-209.
    • (1996) Cell Motil. Cytoskeleton , vol.35 , pp. 200-209
    • Nagaoka, R.1    Abe, H.2    Obinata, T.3
  • 57
    • 0016294918 scopus 로고
    • The measurement of actin concentration in solution: A comparison of methods
    • Houk, T. W. J., and Ue, K. (1974) The measurement of actin concentration in solution: a comparison of methods, Anal. Biochem. 62, 66-74.
    • (1974) Anal. Biochem. , vol.62 , pp. 66-74
    • Houk, T.W.J.1    Ue, K.2
  • 58
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 59
    • 0031443215 scopus 로고    scopus 로고
    • Probing the effects of calcium on gelsolin
    • Pope, B. J., Gooch, J. T., and Weeds, A. G. (1997) Probing the effects of calcium on gelsolin, Biochemistry 36, 15848-15855.
    • (1997) Biochemistry , vol.36 , pp. 15848-15855
    • Pope, B.J.1    Gooch, J.T.2    Weeds, A.G.3
  • 60
    • 0033152592 scopus 로고    scopus 로고
    • 2+ ions to the regulatory binding sites of gelsolin
    • 2+ ions to the regulatory binding sites of gelsolin, Eur. J. Biochem. 262, 330-334.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 330-334
    • Gremm, D.1    Wegner, A.2
  • 61
    • 0020440236 scopus 로고
    • Determination of binding stoichiometry by the continuous variation method: The Job plot
    • Huang, C. Y. (1982) Determination of binding stoichiometry by the continuous variation method: the Job plot, Methods Enzymol. 87, 509-525.
    • (1982) Methods Enzymol. , vol.87 , pp. 509-525
    • Huang, C.Y.1
  • 62
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 63
    • 0024579970 scopus 로고
    • Interactions among serum vitamin D binding protein, monomeric actin, profilin, and profilactin
    • McLeod, J. F., Kowalski, M. A., and Haddad, J. G., Jr. (1989) Interactions among serum vitamin D binding protein, monomeric actin, profilin, and profilactin, J. Biol. Chem. 264, 1260-1267.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1260-1267
    • McLeod, J.F.1    Kowalski, M.A.2    Haddad Jr., J.G.3
  • 64
    • 0033485258 scopus 로고    scopus 로고
    • Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are differentially affected by mutations around the actin-binding helix
    • Moriyama, K., and Yahara, I. (1999) Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are differentially affected by mutations around the actin-binding helix, EMBO J. 18, 6752-6761.
    • (1999) EMBO J. , vol.18 , pp. 6752-6761
    • Moriyama, K.1    Yahara, I.2
  • 65
    • 0021272952 scopus 로고
    • Phalloidin enhances actin assembly by preventing monomer dissociation
    • Coluccio, L. M., and Tilney, L. G. (1984) Phalloidin enhances actin assembly by preventing monomer dissociation, J. Cell Biol. 99, 529-535.
    • (1984) J. Cell Biol. , vol.99 , pp. 529-535
    • Coluccio, L.M.1    Tilney, L.G.2
  • 68
    • 0033597934 scopus 로고    scopus 로고
    • Control of actin filament length and turnover by actin depolymerizing factor (ADF/Cofilin) in the presence of capping proteins and ARP2/3 complex
    • Ressad, F., Didry, D., Egile, C., Pantaloni, D., and Carlier, M. F. (1999) Control of actin filament length and turnover by actin depolymerizing factor (ADF/Cofilin) in the presence of capping proteins and ARP2/3 complex, J. Biol. Chem. 274, 20970-20976.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20970-20976
    • Ressad, F.1    Didry, D.2    Egile, C.3    Pantaloni, D.4    Carlier, M.F.5
  • 69
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard, T. D., and Cooper, J. A. (1986) Actin and actin-binding proteins. A critical evaluation of mechanisms and functions, Annu. Rev. Biochem. 55, 987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 70
    • 0037162424 scopus 로고    scopus 로고
    • Crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution
    • Head, J. F., Swamy, N., and Ray, R. (2002) Crystal structure of the complex between actin and human vitamin D-binding protein at 2.5 A resolution, Biochemistry 41, 9015-9020.
    • (2002) Biochemistry , vol.41 , pp. 9015-9020
    • Head, J.F.1    Swamy, N.2    Ray, R.3
  • 71
    • 0037062405 scopus 로고    scopus 로고
    • Crystal structures of the vitamin D-binding protein and its complex with actin: Structural basis of the actin-scavenger system
    • Otterbein, L. R., Cosio, C., Graceffa, P., and Dominguez, R. (2002) Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system, Proc. Natl. Acad. Sci. U.S.A. 99, 8003-8008.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8003-8008
    • Otterbein, L.R.1    Cosio, C.2    Graceffa, P.3    Dominguez, R.4
  • 72
    • 0032500567 scopus 로고    scopus 로고
    • Cofilin and gelsolin segment-1: Molecular dynamics simulation and biochemical analysis predict a similar actin binding mode
    • Wriggers, W., Tang, J. X., Azuma, T., Marks, P. W., and Janmey, P. A. (1998) Cofilin and gelsolin segment-1: molecular dynamics simulation and biochemical analysis predict a similar actin binding mode, J. Mol. Biol. 282, 921-932.
    • (1998) J. Mol. Biol. , vol.282 , pp. 921-932
    • Wriggers, W.1    Tang, J.X.2    Azuma, T.3    Marks, P.W.4    Janmey, P.A.5
  • 73
    • 0022619258 scopus 로고
    • Purification and characterization of actophorin, a new 15,000-dalton actin-binding protein from Acanthamoeba castellanii
    • Cooper, J. A., Blum, J. D., Williams, R. C. J., and Pollard, T. D. (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, R.C.J.3    Pollard, T.D.4
  • 75
    • 0028069286 scopus 로고
    • The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins
    • McKim, K. S., Matheson, C., Marra, M. A., Wakarchuk, M. F., and Baillie, D. L. (1994) The Caenorhabditis elegans unc-60 gene encodes proteins homologous to a family of actin-binding proteins, Mol. Gen. Genet. 242, 346-357.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 346-357
    • McKim, K.S.1    Matheson, C.2    Marra, M.A.3    Wakarchuk, M.F.4    Baillie, D.L.5
  • 76
    • 0021041789 scopus 로고
    • An actin-depolymerizing protein (depactin) from starfish oocytes: Properties and interaction with actin
    • Mabuchi, I. (1983) An actin-depolymerizing protein (depactin) from starfish oocytes: properties and interaction with actin, J. Cell Biol. 97, 1612-1621.
    • (1983) J. Cell Biol. , vol.97 , pp. 1612-1621
    • Mabuchi, I.1
  • 77
    • 0028921277 scopus 로고
    • Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum
    • Aizawa, H., Sutoh, K., Tsubuki, S., Kawashima, S., Ishii, A., and Yahara, I. (1995) Identification, characterization, and intracellular distribution of cofilin in Dictyostelium discoideum, J. Biol. Chem. 270, 10923-10932.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10923-10932
    • Aizawa, H.1    Sutoh, K.2    Tsubuki, S.3    Kawashima, S.4    Ishii, A.5    Yahara, I.6
  • 78
    • 0029040695 scopus 로고
    • The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound
    • Rosenblatt, J., Peluso, P., and Mitchison, T. J. (1995) The bulk of unpolymerized actin in Xenopus egg extracts is ATP-bound, Mol. Biol. Cell 6, 227-236.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 227-236
    • Rosenblatt, J.1    Peluso, P.2    Mitchison, T.J.3
  • 79
    • 0028357931 scopus 로고
    • Actophorin preferentially binds monomeric ADP-actin over ATP-bound actin: Consequences for cell locomotion
    • Maciver, S. K., and Weeds, A. G. (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
  • 80
    • 0023713668 scopus 로고
    • Identification of two species of actin depolymerizing factor in cultures of BHK cells
    • Koffer, A., Edgar, A. J., and Bamburg, J. R. (1988) Identification of two species of actin depolymerizing factor in cultures of BHK cells, J. Muscle Res. Cell Motil. 9, 320-328.
    • (1988) J. Muscle Res. Cell Motil. , vol.9 , pp. 320-328
    • Koffer, A.1    Edgar, A.J.2    Bamburg, J.R.3
  • 81
    • 0033608731 scopus 로고    scopus 로고
    • A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain
    • Devineni, N., Minamide, L. S., Niu, M., Safer, D., Verma, R., Bamburg, J. R., and Nachmias, V. T. (1999) A quantitative analysis of G-actin binding proteins and the G-actin pool in developing chick brain, Brain Res. 823, 129-140.
    • (1999) Brain Res. , vol.823 , pp. 129-140
    • Devineni, N.1    Minamide, L.S.2    Niu, M.3    Safer, D.4    Verma, R.5    Bamburg, J.R.6    Nachmias, V.T.7
  • 84
    • 0027308310 scopus 로고
    • F-actin content and spatial distribution in resting and chemoattractant-stimulated human polymorphonuclear leucocytes. Which role for intracellular free calcium?
    • Zaffran, Y., Lepidi, H., Bongrand, P., Mege, J. L., and Capo, C. (1993) F-actin content and spatial distribution in resting and chemoattractant-stimulated human polymorphonuclear leucocytes. Which role for intracellular free calcium? J. Cell Sci. 105, 675-684.
    • (1993) J. Cell Sci. , vol.105 , pp. 675-684
    • Zaffran, Y.1    Lepidi, H.2    Bongrand, P.3    Mege, J.L.4    Capo, C.5
  • 85
    • 0020411677 scopus 로고
    • Calcium and magnesium binding to thin and thick filaments in skinned muscle fibres: Electron probe analysis
    • Kitazawa, T., Shuman, H., and Somlyo, A. P. (1982) Calcium and magnesium binding to thin and thick filaments in skinned muscle fibres: electron probe analysis, J. Muscle Res. Cell Motil. 3, 437-454.
    • (1982) J. Muscle Res. Cell Motil. , vol.3 , pp. 437-454
    • Kitazawa, T.1    Shuman, H.2    Somlyo, A.P.3
  • 86
    • 0026514824 scopus 로고
    • Microdomains of high calcium concentration in a presynaptic terminal
    • Llinas, R., Sugimori, M., and Silver, R. B. (1992) Microdomains of high calcium concentration in a presynaptic terminal, Science 256, 677-679.
    • (1992) Science , vol.256 , pp. 677-679
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 87
    • 0030803626 scopus 로고    scopus 로고
    • Spectroscopic study of conformational changes in subdomain 1 of G-actin: Influence of divalent cations
    • Nyitrai, M., Hild, G., Belagyi, J., and Somogyi, B. (1997) Spectroscopic study of conformational changes in subdomain 1 of G-actin: influence of divalent cations, Biophys. J. 73, 2023-2032.
    • (1997) Biophys. J. , vol.73 , pp. 2023-2032
    • Nyitrai, M.1    Hild, G.2    Belagyi, J.3    Somogyi, B.4
  • 88
    • 0033002412 scopus 로고    scopus 로고
    • Water in actin polymerization
    • Fuller, N., and Rand, R. P. (1999) Water in actin polymerization, Biophys. J. 76, 3261-3266.
    • (1999) Biophys. J. , vol.76 , pp. 3261-3266
    • Fuller, N.1    Rand, R.P.2
  • 89
    • 0034113924 scopus 로고    scopus 로고
    • Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents
    • Ichetovkin, I., Han, J., Pang, K. M., Knecht, D. A., and Condeelis, J. S. (2000) Actin filaments are severed by both native and recombinant Dictyostelium cofilin but to different extents, Cell Motil. Cytoskeleton 45, 293-306.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 293-306
    • Ichetovkin, I.1    Han, J.2    Pang, K.M.3    Knecht, D.A.4    Condeelis, J.S.5
  • 90
    • 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, T. D., and Mullins, R. D. (2000) 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
  • 91
    • 0033607682 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility. Role of ADF/cofilin
    • review 62 refs
    • Carlier, M. F., Ressad, F., and Pantaloni, D. (1999) Control of actin dynamics in cell motility. Role of ADF/cofilin, J. Biol. Chem. 274, 33827-33830 (review, 62 refs).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33827-33830
    • Carlier, M.F.1    Ressad, F.2    Pantaloni, D.3
  • 92
    • 0343517587 scopus 로고    scopus 로고
    • PAI-1 stability: The role of histidine residues
    • Mangs, H., Sui, G. C., and Wiman, B. (2000) PAI-1 stability: the role of histidine residues, FEBS Lett. 475, 192-196.
    • (2000) FEBS Lett. , vol.475 , pp. 192-196
    • Mangs, H.1    Sui, G.C.2    Wiman, B.3
  • 93
    • 0032974141 scopus 로고    scopus 로고
    • Design of a pH-dependent cellulose-binding domain
    • Linder, M., Nevanen, T., and Teeri, T. T. (1999) Design of a pH-dependent cellulose-binding domain, FEBS Lett. 447, 13-16.
    • (1999) FEBS Lett. , vol.447 , pp. 13-16
    • Linder, M.1    Nevanen, T.2    Teeri, T.T.3
  • 94
    • 1042289739 scopus 로고    scopus 로고
    • Solution structure of human cofilin: Actin binding, pH sensitivity, and relationship to actin-depolymerizing factor
    • Pope, B. J., Zierler-Gould, K. M., Kuhne, R., Weeds, A. G., and Ball, L. J. (2004) Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor, J. Biol. Chem. 279, 4840-4848.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4840-4848
    • Pope, B.J.1    Zierler-Gould, K.M.2    Kuhne, R.3    Weeds, A.G.4    Ball, L.J.5
  • 96
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • Lappalainen, P., Fedorov, E. V., Fedorov, A. A., Almo, S. C., and Drubin, D. G. (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
  • 97
    • 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, B. J., Tolbert, V. T., Bui, A., Pohl, J., Benian, G. M., Gernert, K. M., and Weeds, A. G. (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
  • 98
    • 0033050852 scopus 로고    scopus 로고
    • XAIP1: A Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins
    • Okada, K., Obinata, T., and Abe, H. (1999) XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins, J. Cell Sci. 112, 1553-1565.
    • (1999) J. Cell Sci. , vol.112 , pp. 1553-1565
    • Okada, K.1    Obinata, T.2    Abe, H.3
  • 99
    • 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, T. D., and Bamburg, J. R. (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
  • 100
    • 0347664159 scopus 로고    scopus 로고
    • Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1
    • Balcer, H. I., Goodman, A. L., Rodal, A. A., Smith, E., Kugler, J., Heuser, J. E., and Goode, B. L. (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
  • 101
    • 0242351058 scopus 로고    scopus 로고
    • Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform
    • Mohri, K., and Ono, S. (2003) Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform, J. Cell Sci. 116, 4107-4118.
    • (2003) J. Cell Sci. , vol.116 , pp. 4107-4118
    • Mohri, K.1    Ono, S.2
  • 102
    • 0030033237 scopus 로고    scopus 로고
    • Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium
    • Aizawa, H., Sutoh, K., and Yahara, I. (1996) Overexpression of cofilin stimulates bundling of actin filaments, membrane ruffling, and cell movement in Dictyostelium, J. Cell Biol. 132, 335-344.
    • (1996) J. Cell Biol. , vol.132 , pp. 335-344
    • Aizawa, H.1    Sutoh, K.2    Yahara, I.3
  • 103
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A. Y., Bailly, M., Zebda, N., Segall, J. E., and Condeelis, J. S. (2000) Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion, J. Cell Biol. 148, 531-542.
    • (2000) J. Cell Biol. , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 104
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/Cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • Zebda, N., Bernard, O., Bailly, M., Welti, S., Lawrence, D. S., and Condeelis, J. S. (2000) Phosphorylation of ADF/Cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension, J. Cell Biol. 151, 1119-1128.
    • (2000) J. Cell Biol. , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6


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