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Volumn 18, Issue 23, 1999, Pages 6752-6761

Two activities of cofilin, severing and accelerating directional depolymerization of actin filaments, are affected differentially by mutations around the actin-binding helix

Author keywords

Actin; Cofilin; Mutation; Tertiary structure; Yeast

Indexed keywords

ACTIN; ALANINE; CARBONYL DERIVATIVE; COFILIN; HYDROXYL GROUP; MUTANT PROTEIN; PHENYLALANINE; SERINE; TYROSINE;

EID: 0033485258     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.23.6752     Document Type: Article
Times cited : (93)

References (44)
  • 1
    • 0029867539 scopus 로고    scopus 로고
    • Xenopus laevis actin-depolymerizing factor/cofilin: A phosphorylation-regulated protein essential for development
    • Abe, H., Obinata, J., 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, J.2    Minamide, L.S.3    Bamburg, J.R.4
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin, L. and Pollard, T.D. (1999) Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem., 274, 15538-15546.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 5
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad, I., Markey, F., Carlsson, L., Persson, T. and Lindberg, U. (1978) Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell, 15, 935-943.
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3    Persson, T.4    Lindberg, U.5
  • 6
    • 0022405144 scopus 로고
    • Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes
    • Bryan, J. and Coluccio, L.M. (1985) Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes. J. Cell Biol., 101, 1236-1244.
    • (1985) J. Cell Biol. , vol.101 , pp. 1236-1244
    • Bryan, J.1    Coluccio, L.M.2
  • 7
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping and nucleation
    • Burtnick, L.D., Koepf, E.K., Grimes, J., Jones, E.Y., Stuart, D.I., McLaughlin, P.J. and Robinson, R.C. (1997) The crystal structure of plasma gelsolin: implications for actin severing, capping and nucleation. Cell, 90, 661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 8
    • 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
  • 9
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry, D., Carlier, M.F. and Pantaloni, D. (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J. Biol. Chem., 273, 25602-25611.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 11
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D. and Sugino, A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 12
    • 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
  • 13
    • 0020004165 scopus 로고
    • The depolymerization of actin by specific proteins from plasma and brain: A quantitative assay
    • Harris, H.E., Bamburg, J.R., Bernstein, B.W. and Weeds, A.G. (1982) The depolymerization of actin by specific proteins from plasma and brain: a quantitative assay. Anal. Biochem., 119, 102-114.
    • (1982) Anal. Biochem. , vol.119 , pp. 102-114
    • Harris, H.E.1    Bamburg, J.R.2    Bernstein, B.W.3    Weeds, A.G.4
  • 14
    • 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. and 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
  • 15
    • 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
  • 16
    • 0032992123 scopus 로고    scopus 로고
    • Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae
    • Iida, K. and Yahara, I. (1999) Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae. Genes Cells, 4, 21-32.
    • (1999) Genes Cells , vol.4 , pp. 21-32
    • Iida, K.1    Yahara, I.2
  • 18
    • 0022969835 scopus 로고
    • Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry and electron microscopy
    • Janmey, P.A., Peetermans, J., Zaner, K.S., Stossel,T.P. and Tanaka, T. (1986) Structure and mobility of actin filaments as measured by quasielastic light scattering, viscometry and electron microscopy. J. Biol. Chem., 261, 8357-8362.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8357-8362
    • Janmey, P.A.1    Peetermans, J.2    Zaner, K.S.3    Tanaka, T.4
  • 19
    • 0030930427 scopus 로고    scopus 로고
    • F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)
    • Jiang, C.J., Weeds, A.G., Khan, S. and Hussey, P.J. (1997) F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF). Proc. Natl Acad. Sci. USA, 94, 9973-9978.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9973-9978
    • Jiang, C.J.1    Weeds, A.G.2    Khan, S.3    Hussey, P.J.4
  • 20
    • 0015374358 scopus 로고
    • A further study of electron microscopic particle length of F-actin polymerized in vitro
    • Kawamura, M. and Maruyama, K. (1972) A further study of electron microscopic particle length of F-actin polymerized in vitro. J. Biochem., 72, 179-188.
    • (1972) J. Biochem. , vol.72 , pp. 179-188
    • Kawamura, M.1    Maruyama, K.2
  • 21
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(l-pyrenyl)-iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama,T. and Mihashi, K. (1981) Fluorimetry study of N-(l-pyrenyl)-iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem., 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Mihashi, K.1
  • 22
    • 0025740912 scopus 로고
    • Improved site-directed mutagenesis method using PCR
    • Kuipers, O.P., Boot, H.J. and de Vos, W.M. (1991) Improved site-directed mutagenesis method using PCR. Nucleic Acids Res., 19, 4558.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4558
    • Kuipers, O.P.1    Boot, H.J.2    De Vos, W.M.3
  • 24
    • 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
  • 26
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • Maciver, S.K., Zot, H.G. and Pollard, T.D. (1991) Characterization of actin filament severing by actophorin from Acanthamoeba castellanii. J. Cell Biol., 115, 1611-1620.
    • (1991) J. Cell Biol. , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 27
    • 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
  • 28
    • 0031879577 scopus 로고    scopus 로고
    • Determination of the gelsolin binding site on F-actin: Implications for severing and capping
    • McGough, A., Chiu, W. and Way, M. (1998) Determination of the gelsolin binding site on F-actin: implications for severing and capping. Biophys. J., 74, 764-772.
    • (1998) Biophys. J. , vol.74 , pp. 764-772
    • McGough, A.1    Chiu, W.2    Way, M.3
  • 29
    • 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
  • 30
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P.J., Gooch, J.T., Mannherz, H.G. and Weeds, A.G. (1993) Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature, 364, 685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 31
    • 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
  • 32
    • 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. and 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
  • 33
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama, K., Iida, K. and 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
  • 34
    • 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
  • 35
    • 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
  • 36
    • 0033519332 scopus 로고    scopus 로고
    • UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle
    • Ono, S., Baillie, D.L. and Benian, G.M. (1999) UNC-60B, an ADF/cofilin family protein, is required for proper assembly of actin into myofibrils in Caenorhabditis elegans body wall muscle. J. Cell Biol., 145, 491-502.
    • (1999) J. Cell Biol. , vol.145 , pp. 491-502
    • Ono, S.1    Baillie, D.L.2    Benian, G.M.3
  • 37
    • 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
  • 39
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A. and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem., 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 41
    • 0028363603 scopus 로고
    • DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments
    • Weber, A., Pennise, C.R. and Pring, M. (1994) DNase I increases the rate constant of depolymerization at the pointed (-) end of actin filaments. Biochemistry, 33, 4780-4786.
    • (1994) Biochemistry , vol.33 , pp. 4780-4786
    • Weber, A.1    Pennise, C.R.2    Pring, M.3
  • 42
    • 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
  • 44
    • 0025744897 scopus 로고
    • Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin
    • Yonezawa, N., Nishida, E., Iida, K., Kumagai, H., Yahara, I. and Sakai, H. (1991) Inhibition of actin polymerization by a synthetic dodecapeptide patterned on the sequence around the actin-binding site of cofilin. J. Biol. Chem., 266, 10485-10489.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10485-10489
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Kumagai, H.4    Yahara, I.5    Sakai, H.6


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