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Volumn 22, Issue 9, 2005, Pages 971-984

Involvement of slingshot in the Rho-mediated dephosphorylation of ADF/cofilin during Xenopus cleavage

Author keywords

Actin filaments; ADF cofilin; Cytokinesis; Slingshot; Xenopus

Indexed keywords

ACTIN; ACTIN DEPOLYMERIZING FACTOR; DEPSIPEPTIDE; JASPAMIDE; PHOSPHOPROTEIN PHOSPHATASE; PRIMER DNA; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 27644482320     PISSN: 02890003     EISSN: 02890003     Source Type: Journal    
DOI: 10.2108/zsj.22.971     Document Type: Article
Times cited : (11)

References (69)
  • 1
    • 0029867539 scopus 로고    scopus 로고
    • Xenopus laevis actin-depolymerizing factor/cofilin: A phosphorylation-regulated protein essential for development
    • Abe H, Obinata T, Minamide LS, Bamburg JR (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
  • 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
  • 3
    • 0035865682 scopus 로고    scopus 로고
    • LIM-kinase 2 induces formation of stress fibers, 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, Mizuno K (2001) LIM-kinase 2 induces formation of stress fibers, 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
  • 4
    • 0037077214 scopus 로고    scopus 로고
    • Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis
    • Amano T, Kaji N, Ohashi K, Mizuno K (2002) Mitosis-specific activation of LIM motif-containing protein kinase and roles of cofilin phosphorylation and dephosphorylation in mitosis. J Biol Chem 277: 22093-22102
    • (2002) J Biol Chem , vol.277 , pp. 22093-22102
    • Amano, T.1    Kaji, N.2    Ohashi, K.3    Mizuno, K.4
  • 5
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach A, Saunus J, Konstandin M, Wesselborg S, Meuer SC, Samstag Y (2000) The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur J Immunol 30: 3422-3431
    • (2000) Eur J Immunol , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 7
    • 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
  • 8
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg JR, McGough A, Ono S (1999) Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol 9: 364-370
    • (1999) Trends Cell Biol , vol.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 10
    • 0033607682 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility. Role of ADF/cofilin
    • Carlier MF, Ressad F, Pantaloni D (1999) Control of actin dynamics in cell motility. Role of ADF/cofilin. J Biol Chem 274: 33827-33830
    • (1999) J Biol Chem , vol.274 , pp. 33827-33830
    • Carlier, M.F.1    Ressad, F.2    Pantaloni, D.3
  • 11
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan AY, Bailly M, Zebda N, Segall JE, Condeelis JS (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
  • 12
    • 0029129581 scopus 로고
    • The murine LIM-kinase gene (limk) encodes a novel serine threonine kinase expressed predominantly in trophoblast giant cells and the developing nervous system
    • Cheng AK, Robertson EJ (1995) The murine LIM-kinase gene (limk) encodes a novel serine threonine kinase expressed predominantly in trophoblast giant cells and the developing nervous system. Mech Dev 52: 187-197
    • (1995) Mech Dev , vol.52 , pp. 187-197
    • Cheng, A.K.1    Robertson, E.J.2
  • 13
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • DesMarais V, Macaluso F, Condeelis J, Bailly M (2004) Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension. J Cell Sci 117: 3499-3510
    • (2004) J Cell Sci , vol.117 , pp. 3499-3510
    • DesMarais, V.1    Macaluso, F.2    Condeelis, J.3    Bailly, M.4
  • 14
    • 0031037187 scopus 로고    scopus 로고
    • A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
    • Drechsel DN, Hyman AA, Hall A, Glotzer M (1997) A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos. Curr Biol 7: 12-23
    • (1997) Curr Biol , vol.7 , pp. 12-23
    • Drechsel, D.N.1    Hyman, A.A.2    Hall, A.3    Glotzer, M.4
  • 15
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards DC, Sanders LC, Bokoch GM, Gill GN (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1: 253-259
    • (1999) Nat Cell Biol , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 16
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh M, Song X, Mouneimne G, Sidani M, Lawrence DS, Condeelis JS (2004) Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304: 743-746
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 17
    • 0035184138 scopus 로고    scopus 로고
    • Animal cell cytokinesis
    • Glotzer M (2001) Animal cell cytokinesis. Annu Rev Cell Dev Biol 17: 351-386
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 351-386
    • Glotzer, M.1
  • 18
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner MW (1991) Cyclin is degraded by the ubiquitin pathway. Nature 349: 132-138
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0042858199 scopus 로고    scopus 로고
    • Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells
    • Kaji N, Ohashi K, Shuin M, Niwa R, Uemura T, Mizuno K (2003) Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells. J Biol Chem 278: 33450-33455
    • (2003) J Biol Chem , vol.278 , pp. 33450-33455
    • Kaji, N.1    Ohashi, K.2    Shuin, M.3    Niwa, R.4    Uemura, T.5    Mizuno, K.6
  • 23
    • 0034625353 scopus 로고    scopus 로고
    • Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation
    • Kimura K, Tsuji T, Takada Y, Miki T, Narumiya S (2000) Accumulation of GTP-bound RhoA during cytokinesis and a critical role of ECT2 in this accumulation. J Biol Chem 275: 17233-17236
    • (2000) J Biol Chem , vol.275 , pp. 17233-17236
    • Kimura, K.1    Tsuji, T.2    Takada, Y.3    Miki, T.4    Narumiya, S.5
  • 24
    • 0027509362 scopus 로고
    • Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI)
    • Kishi K, Sasaki T, Kuroda S, Itoh T, Takai Y (1993) Regulation of cytoplasmic division of Xenopus embryo by rho p21 and its inhibitory GDP/GTP exchange protein (rho GDI). J Cell Biol 120: 1187-1195
    • (1993) J Cell Biol , vol.120 , pp. 1187-1195
    • Kishi, K.1    Sasaki, T.2    Kuroda, S.3    Itoh, T.4    Takai, Y.5
  • 25
    • 0031577728 scopus 로고    scopus 로고
    • cDNA cloning, genomic organization, and chromosomal localization of the mouse LIM-motif-containing kinase gene, Limk2
    • Koshimizu U, Takahashi H, Nakamura T (1997) cDNA cloning, genomic organization, and chromosomal localization of the mouse LIM-motif-containing kinase gene, Limk2. Biochem Biophys Res Commun 241: 243-250
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 243-250
    • Koshimizu, U.1    Takahashi, H.2    Nakamura, T.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 27
    • 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
  • 28
    • 0027691240 scopus 로고
    • A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs
    • Mabuchi I, Hamaguchi Y, Fujimoto H, Morii N, Mishima M, Narumiya S (1993) A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs. Zygote 1: 325-331
    • (1993) Zygote , vol.1 , pp. 325-331
    • Mabuchi, I.1    Hamaguchi, Y.2    Fujimoto, H.3    Morii, N.4    Mishima, M.5    Narumiya, S.6
  • 29
    • 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
  • 30
    • 0036264824 scopus 로고    scopus 로고
    • The ADF/cofilin family: Actin-remodeling proteins
    • reviews 3007
    • Maciver SK, Hussey PJ (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3: reviews 3007. http://genomebiology.eom/2002/3/5/ reviews/3007
    • (2002) Genome Biol , vol.3
    • Maciver, S.K.1    Hussey, P.J.2
  • 32
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg PJ, Ono S, Minamide LS, Takahashi M, Bamburg JR (1998) Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil Cytoskeleton 39: 172-190
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 33
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins. Stimulus-responsive modulators of actin dynamics
    • Moon AL, Drubin DG (1995) The ADF/cofilin proteins. Stimulus-responsive modulators of actin dynamics. Mol Biol Cell 6: 1423-1431
    • (1995) Mol Biol Cell , vol.6 , pp. 1423-1431
    • Moon, A.L.1    Drubin, D.G.2
  • 34
    • 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
  • 36
    • 0026266161 scopus 로고
    • Cell cycle extracts
    • Murray AW (1991) Cell cycle extracts. Methods Cell Biol 36: 581-605
    • (1991) Methods Cell Biol , vol.36 , pp. 581-605
    • Murray, A.W.1
  • 37
    • 0028899043 scopus 로고
    • Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis
    • Nagaoka R, Abe H, Kusano K, Obinata T (1995) Concentration of cofilin, a small actin-binding protein, at the cleavage furrow during cytokinesis. Cell Motil Cytoskeleton 30: 1-7
    • (1995) Cell Motil Cytoskeleton , vol.30 , pp. 1-7
    • Nagaoka, R.1    Abe, H.2    Kusano, K.3    Obinata, T.4
  • 39
    • 0035192626 scopus 로고    scopus 로고
    • Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton
    • Nakano K, Satoh K, Morimatsu A, Ohnuma M, Mabuchi I (2001) Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton. Mol Biol Cell 12: 3515-3526
    • (2001) Mol Biol Cell , vol.12 , pp. 3515-3526
    • Nakano, K.1    Satoh, K.2    Morimatsu, A.3    Ohnuma, M.4    Mabuchi, I.5
  • 40
    • 0042704842 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family
    • Nakano K, Kanai-Azuma M, Kanai Y, Moriyama K, Yazaki K, Hayashi Y, Kitamura N (2003) Cofilin phosphorylation and actin polymerization by NRK/NESK, a member of the germinal center kinase family. Exp Cell Res 287: 219-227
    • (2003) Exp Cell Res , vol.287 , pp. 219-227
    • Nakano, K.1    Kanai-Azuma, M.2    Kanai, Y.3    Moriyama, K.4    Yazaki, K.5    Hayashi, Y.6    Kitamura, N.7
  • 41
    • 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
  • 42
    • 1342346548 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion
    • Nishita M, Wang Y, Tomizawa C, Suzuki A, Niwa R, Uemura T, Mizuno K (2004) Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion. J Biol Chem 279: 7193-7198
    • (2004) J Biol Chem , vol.279 , pp. 7193-7198
    • Nishita, M.1    Wang, Y.2    Tomizawa, C.3    Suzuki, A.4    Niwa, R.5    Uemura, T.6    Mizuno, K.7
  • 43
    • 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
  • 44
    • 0035124103 scopus 로고    scopus 로고
    • Reorganization of actin cytoskeleton at the growing end of the cleavage furrow of Xenopus egg during cytokinesis
    • Noguchi T, Mabuchi I (2001) Reorganization of actin cytoskeleton at the growing end of the cleavage furrow of Xenopus egg during cytokinesis. J Cell Sci 114: 401-412
    • (2001) J Cell Sci , vol.114 , pp. 401-412
    • Noguchi, T.1    Mabuchi, I.2
  • 45
    • 0029088586 scopus 로고
    • LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family
    • Nunoue K, Ohashi K, Okano I, Mizuno K (1995) LIMK-1 and LIMK-2, two members of a LIM motif-containing protein kinase family. Oncogene 11: 701-710
    • (1995) Oncogene , vol.11 , pp. 701-710
    • Nunoue, K.1    Ohashi, K.2    Okano, I.3    Mizuno, K.4
  • 46
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell PZ, Goodman HM, O'Farrell PH (1977) High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12: 1133-1141
    • (1977) Cell , vol.12 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 47
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • Ohashi K, Nagata K, Maekawa M, Ishizaki T, Narumiya S, Mizuno K (2000) Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J Biol Chem 275: 3577-3582
    • (2000) J Biol Chem , vol.275 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 48
    • 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, Mizuno K, Takeichi M (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    Takeichi, M.10
  • 49
    • 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, 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
  • 50
    • 0029594144 scopus 로고
    • Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs
    • Okano I, Hiraoka J, Otera H, Nunoue K, Ohashi K, Iwashita S, Hirai M, Mizuno K (1995) Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J Biol Chem 270: 31321-31330
    • (1995) J Biol Chem , vol.270 , pp. 31321-31330
    • Okano, I.1    Hiraoka, J.2    Otera, H.3    Nunoue, K.4    Ohashi, K.5    Iwashita, S.6    Hirai, M.7    Mizuno, K.8
  • 52
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pelham RJ, Chang F (2002) Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419: 82-86
    • (2002) Nature , vol.419 , pp. 82-86
    • Pelham, R.J.1    Chang, F.2
  • 53
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112: 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 54
    • 0033200353 scopus 로고    scopus 로고
    • A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila
    • Prokopenko SN, Brumby A, O'Keefe L, Prior L, He Y, Saint R, Bellen HJ (1999) A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila. Genes Dev 13: 2301-2314
    • (1999) Genes Dev , vol.13 , pp. 2301-2314
    • Prokopenko, S.N.1    Brumby, A.2    O'Keefe, L.3    Prior, L.4    He, Y.5    Saint, R.6    Bellen, H.J.7
  • 55
    • 0029164774 scopus 로고
    • Purification of recombinant Rho/Rac/G25K from Escherichia coli
    • Self AJ, Hall A (1995) Purification of recombinant Rho/Rac/G25K from Escherichia coli. Methods Enzymol 256: 3-10
    • (1995) Methods Enzymol , vol.256 , pp. 3-10
    • Self, A.J.1    Hall, A.2
  • 56
    • 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 JA, 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
  • 57
    • 0033611107 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho-and Cdc42-activated LIM-kinase 2
    • Sumi T, Matsumoto K, Takai Y, Nakamura T (1999) Cofilin phosphorylation and actin cytoskeletal dynamics regulated by rho-and Cdc42-activated 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
  • 58
    • 0035808419 scopus 로고    scopus 로고
    • Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase
    • Sumi T, Matsumoto K, Nakamura T (2001a) Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem 276: 670-676
    • (2001) J Biol Chem , vol.276 , pp. 670-676
    • Sumi, T.1    Matsumoto, K.2    Nakamura, T.3
  • 59
    • 0035933849 scopus 로고    scopus 로고
    • Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha
    • Sumi T, Matsumoto K, Shibuya A, Nakamura T (2001b) Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. J Biol Chem 276: 23092-23096
    • (2001) J Biol Chem , vol.276 , pp. 23092-23096
    • Sumi, T.1    Matsumoto, K.2    Shibuya, A.3    Nakamura, T.4
  • 60
    • 0030910515 scopus 로고    scopus 로고
    • Xenopus LIM motif-containing protein kinase, Xlimk1, is expressed in the developing head structure of the embryo
    • Takahashi T, Aoki S, Nakamura T, Koshimizu U, Matsumoto K, Nakamura T (1997) Xenopus LIM motif-containing protein kinase, Xlimk1, is expressed in the developing head structure of the embryo. Dev Dyn 209: 196-205
    • (1997) Dev Dyn , vol.209 , pp. 196-205
    • Takahashi, T.1    Aoki, S.2    Nakamura, T.3    Koshimizu, U.4    Matsumoto, K.5    Nakamura, T.6
  • 61
    • 0035862811 scopus 로고    scopus 로고
    • Functional involvement of Xenopus LIM kinases in progression of oocyte maturation
    • Takahashi T, Koshimizu U, Abe H, Obinata T, Nakamura T (2001) Functional involvement of Xenopus LIM kinases in progression of oocyte maturation. Dev Biol 229: 554-567
    • (2001) Dev Biol , vol.229 , pp. 554-567
    • Takahashi, T.1    Koshimizu, U.2    Abe, H.3    Obinata, T.4    Nakamura, T.5
  • 62
    • 0029131982 scopus 로고
    • Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi K, Sasaki T, Kameyama T, Tsukita S, Takai Y (1995) Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene 11: 39-48
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Takai, Y.5
  • 63
    • 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 JY, Amano T, Yang N, Narumiya S, Mizuno K (2001a) 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
  • 64
    • 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 JY, Takeuchi K, Mori R, Mizuno K (2001b) 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
  • 65
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • USA
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 66
  • 68
    • 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 DS, Condeelis JS (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
  • 69
    • 12244262321 scopus 로고    scopus 로고
    • Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils
    • Zhan Q, Bamburg JR, Badwey JA (2003) Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils. Cell Motil Cytoskeleton 54: 1-15
    • (2003) Cell Motil Cytoskeleton , vol.54 , pp. 1-15
    • Zhan, Q.1    Bamburg, J.R.2    Badwey, J.A.3


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