메뉴 건너뛰기




Volumn 118, Issue 1, 2005, Pages 19-26

Cofilin takes the lead

Author keywords

Arp2 3 complex; Chemotaxis; Stimulated protrusion model

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; CALCINEURIN; COFILIN; F ACTIN; G ACTIN; GELSOLIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C GAMMA; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; PROFILIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; TROPOMYOSIN;

EID: 14044277430     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01631     Document Type: Article
Times cited : (255)

References (88)
  • 1
    • 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
  • 2
    • 0032803529 scopus 로고    scopus 로고
    • Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin
    • Aizawa, H., Katadae, M., Maruya, M., Sameshima, M., Murakami-Murofushi, K. and Yahara, I. (1999). Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin. Genes Cells 4, 311-324.
    • (1999) Genes Cells , vol.4 , pp. 311-324
    • Aizawa, H.1    Katadae, M.2    Maruya, M.3    Sameshima, M.4    Murakami-Murofushi, K.5    Yahara, I.6
  • 3
    • 0242441610 scopus 로고    scopus 로고
    • Actin filament uncapping localizes to ruffling lamellae and rocketing vesicles
    • Allen, P. G. (2003). Actin filament uncapping localizes to ruffling lamellae and rocketing vesicles. Nat. Cell Biol. 5 972-979.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 972-979
    • Allen, P.G.1
  • 4
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann, K. J. and Pollard, T. D. (2001). Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. USA 98, 15009-15013.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 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, S. C. and 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
    • 0032473498 scopus 로고    scopus 로고
    • Gelsolin is a downstream effector of rac for fibroblast motility
    • Azuma, T., Witke, W., Stossel, T. P., Hartwig, J. H. and Kwiatkowski, D. J. (1998). Gelsolin is a downstream effector of rac for fibroblast motility. EMBO J. 17, 1362-1370.
    • (1998) EMBO J. , vol.17 , pp. 1362-1370
    • Azuma, T.1    Witke, W.2    Stossel, T.P.3    Hartwig, J.H.4    Kwiatkowski, D.J.5
  • 8
    • 0344299281 scopus 로고    scopus 로고
    • Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation
    • Bailly, M., Macaluso, F., Cammer, M., Chan, A., Segall, J. E. and Condeelis, J. S. (1999). Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation. J. Cell Biol. 145, 331-345.
    • (1999) J. Cell Biol. , vol.145 , pp. 331-345
    • Bailly, M.1    Macaluso, F.2    Cammer, M.3    Chan, A.4    Segall, J.E.5    Condeelis, J.S.6
  • 9
    • 0035901569 scopus 로고    scopus 로고
    • The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension
    • Bailly, M., Ichetovkin, I., Grant, W., Zebda, N., Machesky, L. M., Segall, J. E. and Condeelis, J. (2001). The F-actin side binding activity of the Arp2/3 complex is essential for actin nucleation and lamellipod extension. Curr. Biol. 11, 620-625.
    • (2001) Curr. Biol. , vol.11 , pp. 620-625
    • Bailly, M.1    Ichetovkin, I.2    Grant, W.3    Zebda, N.4    Machesky, L.M.5    Segall, J.E.6    Condeelis, J.7
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 14
    • 2342514815 scopus 로고    scopus 로고
    • Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells
    • Bertling, E., Hotulainen, P., Mattila, P. K., Matilainen, T., Salminen, M. and 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
  • 15
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin, L., Amann, K. J., Higgs, H. N., Marchand, J. B., Kaiser, D. A. and Pollard, T. D. (2000). Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007-1011.
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 16
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • Blanchoin, L., Pollard, T. D. and Hitchcock-DeGregori, S. E. (2001). Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Curr. Biol. 11, 1300-1304.
    • (2001) Curr. Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-DeGregori, S.E.3
  • 18
    • 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
  • 19
    • 0031908252 scopus 로고    scopus 로고
    • EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells
    • Chan, A. Y., Raft, S., Bailly, M., Wyckoff, J. B., Segall, J. E. and Condeelis, J. S. (1998). EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells. J. Cell Sci. 111, 199-211.
    • (1998) J. Cell Sci. , vol.111 , pp. 199-211
    • Chan, A.Y.1    Raft, S.2    Bailly, M.3    Wyckoff, J.B.4    Segall, J.E.5    Condeelis, J.S.6
  • 20
    • 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
  • 22
    • 0036231070 scopus 로고    scopus 로고
    • Distribution of gelsolin and pbosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility
    • Chou, J., Stolz, D. B., Burke, N. A., Watkins, S. C. and Wells, A. (2002). Distribution of gelsolin and pbosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility. Int. J. Biochem. Cell Biol. 34, 776-790.
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 776-790
    • Chou, J.1    Stolz, D.B.2    Burke, N.A.3    Watkins, S.C.4    Wells, A.5
  • 23
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis, J. (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.1
  • 25
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: Tropomyosin provides stability
    • Cooper, J. A. (2002). Actin dynamics: tropomyosin provides stability. Curr. Biol. 12, R523-R525.
    • (2002) Curr. Biol. , vol.12
    • Cooper, J.A.1
  • 26
    • 0026570396 scopus 로고
    • Targeted disruption of the ABP-120 gene leads to cells with altered motility
    • Cox, D., Condeelis, J., Wessels, D., Soll, D., Kern, H. and Knecht, D. A. (1992). Targeted disruption of the ABP-120 gene leads to cells with altered motility. J. Cell Biol. 116, 943-955.
    • (1992) J. Cell Biol. , vol.116 , pp. 943-955
    • Cox, D.1    Condeelis, J.2    Wessels, D.3    Soll, D.4    Kern, H.5    Knecht, D.A.6
  • 27
    • 0033533744 scopus 로고    scopus 로고
    • Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide
    • Cramer, L. P. (1999). Role of actin-filament disassembly in lamellipodium protrusion in motile cells revealed using the drug jasplakinolide. Curr. Biol. 9, 1095-1105.
    • (1999) Curr. Biol. , vol.9 , pp. 1095-1105
    • Cramer, L.P.1
  • 28
    • 0035943704 scopus 로고    scopus 로고
    • Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin
    • Dan, C., Kelly, A., Bernard, O. and Minden, A. (2001). Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J. Biol. Chem. 276, 32115-32121.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32115-32121
    • Dan, C.1    Kelly, A.2    Bernard, O.3    Minden, A.4
  • 29
    • 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
  • 30
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • DesMarais, V., Ichetovkin, I., Condeelis, J. and Hitchcock-DeGregori, S. E. (2002). Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J. Cell Sci. 115, 4649-4660.
    • (2002) J. Cell Sci. , vol.115 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 31
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • DesMarais, V., Macaluso, F., Condeelis, J. and 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
  • 33
    • 0032558437 scopus 로고    scopus 로고
    • Kinetic studies on the effect of yeast cofilin on yeast actin polymerization
    • Du, J. and Frieden, C. (1998). Kinetic studies on the effect of yeast cofilin on yeast actin polymerization. Biochemistry 37, 13276-13284.
    • (1998) Biochemistry , vol.37 , pp. 13276-13284
    • Du, J.1    Frieden, C.2
  • 34
    • 0030728491 scopus 로고    scopus 로고
    • Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium
    • Eddy, R. J., Han, J. and Condeelis, J. S. (1997). Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium. J. Cell Biol. 139, 1243-1253.
    • (1997) J. Cell Biol. , vol.139 , pp. 1243-1253
    • Eddy, R.J.1    Han, J.2    Condeelis, J.S.3
  • 35
    • 0029911314 scopus 로고    scopus 로고
    • Elongation factor-1 alpha is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma
    • Edmonds, B. T., Wyckoff, J., Yeung, Y. G., Wang, Y., Stanley, E. R., Jones, J., Segall, J. and Condeelis, J. (1996). Elongation factor-1 alpha is an overexpressed actin binding protein in metastatic rat mammary adenocarcinoma. J. Cell Sci. 109, 2705-2714.
    • (1996) J. Cell Sci. , vol.109 , pp. 2705-2714
    • Edmonds, B.T.1    Wyckoff, J.2    Yeung, Y.G.3    Wang, Y.4    Stanley, E.R.5    Jones, J.6    Segall, J.7    Condeelis, J.8
  • 36
    • 0037389872 scopus 로고    scopus 로고
    • Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin
    • Endo, M., Ohashi, K., Sasaki, Y., Goshima, Y., Niwa, R., Uemura, T. and Mizuno, K. (2003). Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin. J. Neurosci. 23, 2527-2537.
    • (2003) J. Neurosci. , vol.23 , pp. 2527-2537
    • Endo, M.1    Ohashi, K.2    Sasaki, Y.3    Goshima, Y.4    Niwa, R.5    Uemura, T.6    Mizuno, K.7
  • 37
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • Evangelista, M., Zigmond, S. and Boone, C. (2003). Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116, 2603-2611.
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 38
    • 0034554857 scopus 로고    scopus 로고
    • Roles of SLP-76, phosphoinositide 3-kinase, and gelsolin in the platelet shape changes initiated by the collagen receptor GPVI/FcR gamma-chain complex
    • Falet, H., Barkalow, K. L., Pivniouk, V. I., Barnes, M. J., Geha, R. S. and Hartwig, J. H. (2000). Roles of SLP-76, phosphoinositide 3-kinase, and gelsolin in the platelet shape changes initiated by the collagen receptor GPVI/FcR gamma-chain complex. Blood 96, 3786-3792.
    • (2000) Blood , vol.96 , pp. 3786-3792
    • Falet, H.1    Barkalow, K.L.2    Pivniouk, V.I.3    Barnes, M.J.4    Geha, R.S.5    Hartwig, J.H.6
  • 40
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto, S., Meili, R., Lee, S., Parry, L. and Firtel, R. A. (2002). Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 109, 611-623.
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 41
    • 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, D. S. and Condeelis, J. S. (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
  • 42
    • 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
  • 43
    • 0025760751 scopus 로고
    • Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation
    • Goldschmidt-Clermont, P. J., Kim, J. W., Machesky, L. M., Rhee, S. G. and Pollard, T. D. (1991). Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation. Science 251 1231-1233.
    • (1991) Science , vol.251 , pp. 1231-1233
    • Goldschmidt-Clermont, P.J.1    Kim, J.W.2    Machesky, L.M.3    Rhee, S.G.4    Pollard, T.D.5
  • 44
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont, P. J., Furman, M. I., Wachsstock, D., Safer, D., Nachmias, V. T. and Pollard, T. D. (1992). The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol. Biol. Cell 3, 1015-1024.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 45
    • 0024453412 scopus 로고
    • Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: Their regulation by chemotactic stimulation
    • Hall, A. L., Warren, V., Dharmawardhane, S. and Condeelis, J. (1989). Identification of actin nucleation activity and polymerization inhibitor in ameboid cells: their regulation by chemotactic stimulation. J. Cell Biol. 109, 2207-2213.
    • (1989) J. Cell Biol. , vol.109 , pp. 2207-2213
    • Hall, A.L.1    Warren, V.2    Dharmawardhane, S.3    Condeelis, J.4
  • 46
    • 0030067632 scopus 로고    scopus 로고
    • Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon
    • Hammell, R. L. and Hitchcock-DeGregori, S. E. (1996). Mapping the functional domains within the carboxyl terminus of alpha-tropomyosin encoded by the alternatively spliced ninth exon. J. Biol. Chem. 271, 4236-4242.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4236-4242
    • Hammell, R.L.1    Hitchcock-DeGregori, S.E.2
  • 47
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., Bokoch, G. M., Carpenter, C. L., Janmey, P. A., Taylor, L. A., Toker, A. and Stossel, T. P. (1995). Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 48
    • 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
  • 49
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs, H. N. and Pollard, T. D. (2001). Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70, 649-676.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 50
    • 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
  • 51
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin, I., Grant, W. and Condeelis, J. (2002). Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12, 79-84.
    • (2002) Curr. Biol. , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 52
    • 0037205230 scopus 로고    scopus 로고
    • Tumor suppressor PTEN mediates sensing of chemoattractant gradients
    • Iijima, M. and Devreotes, P. (2002). Tumor suppressor PTEN mediates sensing of chemoattractant gradients. Cell 109, 599-610.
    • (2002) Cell , vol.109 , pp. 599-610
    • Iijima, M.1    Devreotes, P.2
  • 53
    • 0028935030 scopus 로고
    • Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins
    • Kanamori, T., Hayakawa, T., Suzuki, M. and Titani, K. (1995). Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon beta-adrenergic stimulation, as destrin- and cofilin-like proteins. J. Biol. Chem. 270, 8061-8067.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8061-8067
    • Kanamori, T.1    Hayakawa, T.2    Suzuki, M.3    Titani, K.4
  • 54
  • 55
    • 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
  • 56
    • 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 Cartier, 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    Cartier, M.F.4
  • 57
    • 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
  • 58
    • 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
  • 59
    • 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
  • 60
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P. J., Ono, S., Minamide, L. S., Takahashi, M. and Bamburg, J. R. (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
  • 61
    • 0037093266 scopus 로고    scopus 로고
    • Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover
    • Moriyama, K. and Yahara, I. (2002). Human CAP1 is a key factor in the recycling of cofilin and actin for rapid actin turnover. J. Cell Sci. 115, 1591-1601.
    • (2002) J. Cell Sci. , vol.115 , pp. 1591-1601
    • Moriyama, K.1    Yahara, I.2
  • 62
    • 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
  • 64
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R. D., Heuser, J. A. and Pollard, T. D. (1998). The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95, 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 65
    • 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
  • 66
    • 0035951069 scopus 로고    scopus 로고
    • Identification of yeast cofilin residues specific for actin monomer and PIP2 binding
    • Ojala, P. J., Paavilainen, V. and 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
  • 67
    • 0030601313 scopus 로고    scopus 로고
    • Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood
    • Okada, K., Takano-Ohmuro, H., Obinata, T. and Abe, H. (1996). Dephosphorylation of cofilin in polymorphonuclear leukocytes derived from peripheral blood. Exp. Cell Res. 227, 116-122.
    • (1996) Exp. Cell Res. , vol.227 , pp. 116-122
    • Okada, K.1    Takano-Ohmuro, H.2    Obinata, T.3    Abe, H.4
  • 68
    • 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
  • 69
    • 0344391975 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1, new blades for twisted filaments
    • Ono, S. (2003). Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1, new blades for twisted filaments. Biochemistry 42, 13363-13370.
    • (2003) Biochemistry , vol.42 , pp. 13363-13370
    • Ono, S.1
  • 70
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono, S. and 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
  • 71
    • 0033771755 scopus 로고    scopus 로고
    • The Arp2/3 complex branches filament barbed ends: Functional antagonism with capping proteins
    • Pantaloni, D., Boujemaa, R., Didry, D., Gounon, P. and Carlier, M. F. (2000). The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins. Nat. Cell Biol. 2, 385-391.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 385-391
    • Pantaloni, D.1    Boujemaa, R.2    Didry, D.3    Gounon, P.4    Carlier, M.F.5
  • 72
    • 0038064201 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D. and Borisy, G. G. (2003). Cellular motility driven by assembly and disassembly of actin filaments. Cell 113, 549.
    • (2003) Cell , vol.113 , pp. 549
    • Pollard, T.D.1    Borisy, G.G.2
  • 73
    • 0033895234 scopus 로고    scopus 로고
    • Molecular mechanisms controlling actin filament dynamics in nonmuscle cells
    • Pollard, T. D., Blanchoin, L. and Mullins, R. D. (2000). Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545-576.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 545-576
    • Pollard, T.D.1    Blanchoin, L.2    Mullins, R.D.3
  • 74
  • 76
    • 0032853684 scopus 로고    scopus 로고
    • Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis
    • Rosok, O., Pedeutour, F., Ree, A. H. and Aasheim, H. C. (1999). Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis. Genomics 61, 44-54.
    • (1999) Genomics , vol.61 , pp. 44-54
    • Rosok, O.1    Pedeutour, F.2    Ree, A.H.3    Aasheim, H.C.4
  • 78
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multifunctional actin regulatory protein
    • Sun, H. Q., Yamamoto, M., Mejillano, M. and Yin, H. L. (1999). Gelsolin, a multifunctional actin regulatory protein. J. Biol. Chem. 274, 33179-33182.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 80
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M. and Borisy, G. G. (1999). Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 81
    • 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
  • 83
    • 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
  • 84
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa, N., Nishida, E. and Sakai, H. (1985). pH control of actin polymerization by cofilin. J. Biol. Chem. 260 14410-14412.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 85
    • 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
  • 86
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa, N., Homma, Y., Yahara, I., Sakai, H. and Nishida, E. (1991). A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266, 17218-17221.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 87
    • 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
  • 88
    • 12244262321 scopus 로고    scopus 로고
    • Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils
    • Zhan, Q., Bamburg, J. R. and Badwey, J. A. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.