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Volumn 62, Issue 9, 2005, Pages 955-970

Actin polymerization machinery: The finish line of signaling networks, the starting point of cellular movement

Author keywords

Actin dynamics; Actin binding proteins; Lamellipodia; RhoGTPases; Signaling complex

Indexed keywords

ACTIN BINDING PROTEIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; COFILIN; G ACTIN; GELSOLIN; GROWTH FACTOR; MONOMER; NAP1 PROTEIN; PROFILIN; PROTEIN; PROTEIN ABI; PROTEIN EPS8; PROTEIN TYROSINE KINASE; RAC PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SOS PROTEIN; UNCLASSIFIED DRUG;

EID: 18544379580     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-004-4472-6     Document Type: Review
Times cited : (133)

References (161)
  • 1
    • 0037459075 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 112(4): 453-465
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 3
    • 0035947404 scopus 로고    scopus 로고
    • Mechanism of actin-based motility
    • Pantaloni D., Le Clainche C. and Carlier M. F. (2001) Mechanism of actin-based motility. Science 292(5521): 1502-1506
    • (2001) Science , vol.292 , Issue.5521 , pp. 1502-1506
    • Pantaloni, D.1    Le Clainche, C.2    Carlier, M.F.3
  • 4
    • 0033772741 scopus 로고    scopus 로고
    • Actin assembly mediated by Arp2/3 complex and WASP family proteins
    • Mullins R. D. and Machesky L. M. (2000) Actin assembly mediated by Arp2/3 complex and WASP family proteins. Methods Enzymol. 325: 214-237
    • (2000) Methods Enzymol. , vol.325 , pp. 214-237
    • Mullins, R.D.1    Machesky, L.M.2
  • 5
    • 0033545605 scopus 로고    scopus 로고
    • Actin polymerization: Where the WASP stings
    • Bi E. and Zigmond S. H. (1999) Actin polymerization: where the WASP stings. Curr. Biol. 9(5): R160-163
    • (1999) Curr. Biol. , vol.9 , Issue.5
    • Bi, E.1    Zigmond, S.H.2
  • 6
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. (1998) Rho GTPases and the actin cytoskeleton. Science 279(5350): 509-514
    • (1998) Science , vol.279 , Issue.5350 , pp. 509-514
    • Hall, A.1
  • 7
    • 0025970527 scopus 로고
    • Actin: Protein structure and filament dynamics
    • Carlier M. F. (1991) Actin: protein structure and filament dynamics. J. Biol. Chem. 266(1): 1-4
    • (1991) J. Biol. Chem. , vol.266 , Issue.1 , pp. 1-4
    • Carlier, M.F.1
  • 8
    • 0025753377 scopus 로고
    • Nucleotide hydrolysis in cytoskeletal assembly
    • Carlier M. F. (1991) Nucleotide hydrolysis in cytoskeletal assembly. Curr. Opin. Cell Biol. 3(1): 12-17
    • (1991) Curr. Opin. Cell Biol. , vol.3 , Issue.1 , pp. 12-17
    • Carlier, M.F.1
  • 9
    • 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(2): 331-345
    • (1999) J. Cell Biol. , vol.145 , Issue.2 , pp. 331-345
    • Bailly, M.1    Macaluso, F.2    Cammer, M.3    Chan, A.4    Segall, J.E.5    Condeelis, J.S.6
  • 10
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang Y. L. (1985) Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J. Cell Biol. 101(2): 597-602
    • (1985) J. Cell Biol. , vol.101 , Issue.2 , pp. 597-602
    • Wang, Y.L.1
  • 11
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • Small J. V., Isenberg G. and Celis J. E. (1978) Polarity of actin at the leading edge of cultured cells. Nature 272(5654): 638-639
    • (1978) Nature , vol.272 , Issue.5654 , pp. 638-639
    • Small, J.V.1    Isenberg, G.2    Celis, J.E.3
  • 12
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch M. D., Rosenblatt J., Skoble J., Portnoy D. A. and Mitchison T. J. (1998) Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281(5373): 105-108
    • (1998) Science , vol.281 , Issue.5373 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 13
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch M. D., Iwamatsu A. and Mitchison T. J. (1997) Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385(6613): 265-269
    • (1997) Nature , vol.385 , Issue.6613 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 14
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile C., Loisel T. P., Laurent V., Li R., Pantaloni D., Sansonetti P. J. et al. (1999) Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146(6): 1319-1332
    • (1999) J. Cell Biol. , vol.146 , Issue.6 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6
  • 15
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • Theriot J. A., Mitchison T. J., Tilney L. G. and Portnoy D. A. (1992) The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357(6375): 257-260
    • (1992) Nature , vol.357 , Issue.6375 , pp. 257-260
    • Theriot, J.A.1    Mitchison, T.J.2    Tilney, L.G.3    Portnoy, D.A.4
  • 16
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly
    • Dabiri G. A., Sanger J. M., Portnoy D. A. and Southwick F. S. (1990) Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc. Natl. Acad. Sci. USA 87(16): 6068-6072
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.16 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 17
    • 0032006817 scopus 로고    scopus 로고
    • Control of actin dynamics
    • Carlier M. F. (1998) Control of actin dynamics. Curr. Opin. Cell Biol. 10(1): 45-51
    • (1998) Curr. Opin. Cell Biol. , vol.10 , Issue.1 , pp. 45-51
    • Carlier, M.F.1
  • 18
    • 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
  • 19
    • 0037415575 scopus 로고    scopus 로고
    • A biomimetic motility assay provides insight into the mechanism of actin-based motility
    • Wiesner S., Helfer E., Didry D., Ducouret G., Lafuma F., Carlier M. F. et al. (2003) A biomimetic motility assay provides insight into the mechanism of actin-based motility. J. Cell Biol. 160(3): 387-398
    • (2003) J. Cell Biol. , vol.160 , Issue.3 , pp. 387-398
    • Wiesner, S.1    Helfer, E.2    Didry, D.3    Ducouret, G.4    Lafuma, F.5    Carlier, M.F.6
  • 20
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • Yarar D., To W., Abo A. and Welch M. D. (1999) The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9(10): 555-558
    • (1999) Curr. Biol. , vol.9 , Issue.10 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4
  • 21
    • 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(6753): 613-616
    • (1999) Nature , vol.401 , Issue.6753 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 22
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • Rogers S. L., Wiedemann U., Stuurman N. and Vale R. D. (2003) Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J. Cell Biol. 162(6): 1079-1088
    • (2003) J. Cell Biol. , vol.162 , Issue.6 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 23
  • 24
    • 0028839660 scopus 로고
    • The ADF/cofilin proteins: Stimulus-responsive modulators of actin dynamics
    • Moon A. and Drubin D. G. (1995) The ADF/cofilin proteins: stimulus-responsive modulators of actin dynamics. Mol. Biol. Cell 6(11): 1423-1431
    • (1995) Mol. Biol. Cell , vol.6 , Issue.11 , pp. 1423-1431
    • Moon, A.1    Drubin, D.G.2
  • 25
    • 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(7): 288-293
    • (2001) Trends Cell Biol. , vol.11 , Issue.7 , pp. 288-293
    • Condeelis, J.1
  • 26
    • 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. et al. (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136(6): 1307-1322
    • (1997) J. Cell Biol. , vol.136 , Issue.6 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6
  • 27
    • 0029859963 scopus 로고    scopus 로고
    • Dephosphorylation of serine 3 regulates nuclear translocation of cofilin
    • Nebl G., Meuer S. C. and Samstag Y. (1996) Dephosphorylation of serine 3 regulates nuclear translocation of cofilin. J. Biol. Chem. 271(42): 26276-26280
    • (1996) J. Biol. Chem. , vol.271 , Issue.42 , pp. 26276-26280
    • Nebl, G.1    Meuer, S.C.2    Samstag, Y.3
  • 28
    • 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
  • 29
    • 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(2): 233-246
    • (2002) Cell , vol.108 , Issue.2 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 30
    • 2542421811 scopus 로고    scopus 로고
    • The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly
    • Hertzog M., van Heijenoort C., Didry D., Gaudier M., Coutant J., Gigant B. et al. (2004) The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117(5): 611-623
    • (2004) Cell , vol.117 , Issue.5 , pp. 611-623
    • Hertzog, M.1    Van Heijenoort, C.2    Didry, D.3    Gaudier, M.4    Coutant, J.5    Gigant, B.6
  • 31
    • 0034664732 scopus 로고    scopus 로고
    • Ciboulot regulates actin assembly during Drosophila brain metamorphosis
    • Boquet I., Boujemaa R., Carlier M. F. and Preat T. (2000) Ciboulot regulates actin assembly during Drosophila brain metamorphosis. Cell 102(6): 797-808
    • (2000) Cell , vol.102 , Issue.6 , pp. 797-808
    • Boquet, I.1    Boujemaa, R.2    Carlier, M.F.3    Preat, T.4
  • 32
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D. and Carlier M. F. (1993) How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 75(5): 1007-1014
    • (1993) Cell , vol.75 , Issue.5 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 33
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard T. D. and Cooper J. A. (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23(26): 6631-6641
    • (1984) Biochemistry , vol.23 , Issue.26 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 34
    • 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(40): 25602-25611
    • (1998) J. Biol. Chem. , vol.273 , Issue.40 , pp. 25602-25611
    • Didry, D.1    Carlier, M.F.2    Pantaloni, D.3
  • 35
    • 0029065328 scopus 로고
    • Capping protein levels influence actin assembly and cell motility in dictyostelium
    • Hug C., Jay P. Y., Reddy I., McNally J. G., Bridgman P. C., Elson E. L. et al. (1995) Capping protein levels influence actin assembly and cell motility in dictyostelium. Cell 81(4): 591-600
    • (1995) Cell , vol.81 , Issue.4 , pp. 591-600
    • Hug, C.1    Jay, P.Y.2    Reddy, I.3    McNally, J.G.4    Bridgman, P.C.5    Elson, E.L.6
  • 36
    • 0028941257 scopus 로고
    • Effects of CapG overexpression on agonist-induced motility and second messenger generation
    • Sun H. Q., Kwiatkowska K., Wooten D. C. and Yin H. L. (1995) Effects of CapG overexpression on agonist-induced motility and second messenger generation. J. Cell Biol. 129(1): 147-156
    • (1995) J. Cell Biol. , vol.129 , Issue.1 , pp. 147-156
    • Sun, H.Q.1    Kwiatkowska, K.2    Wooten, D.C.3    Yin, H.L.4
  • 37
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: New insights into mechanism and regulation
    • Wear M. A. and Cooper J. A. (2004) Capping protein: new insights into mechanism and regulation. Trends Biochem. Sci. 29(8): 418-428
    • (2004) Trends Biochem. Sci. , vol.29 , Issue.8 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 39
    • 0032702258 scopus 로고    scopus 로고
    • Proteins that regulate dynamic actin remodeling in response to membrane signaling minireview series
    • Yin H. L. and Stull J. T. (1999) Proteins that regulate dynamic actin remodeling in response to membrane signaling minireview series. J. Biol. Chem. 274(46): 32529-32530
    • (1999) J. Biol. Chem. , vol.274 , Issue.46 , pp. 32529-32530
    • Yin, H.L.1    Stull, J.T.2
  • 40
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end
    • Mejillano M. R., Kojima S., Applewhite D. A., Gertler F. B., Svitkina T. M. and Borisy G. G. (2003) Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 118(3): 363-373
    • (2003) Cell , vol.118 , Issue.3 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5    Borisy, G.G.6
  • 41
    • 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(11): 972-979
    • (2003) Nat. Cell Biol. , vol.5 , Issue.11 , pp. 972-979
    • Allen, P.G.1
  • 42
    • 0036231070 scopus 로고    scopus 로고
    • Distribution of gelsolin and phosphoinositol 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 phosphoinositol 4,5-bisphosphate in lamellipodia during EGF-induced motility. Int. J. Biochem. Cell Biol. 34(7): 776-790
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , Issue.7 , pp. 776-790
    • Chou, J.1    Stolz, D.B.2    Burke, N.A.3    Watkins, S.C.4    Wells, A.5
  • 43
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates
    • Schafer D. A., Korshunova Y. O., Schroer T. A. and Cooper J. A. (1994) Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates. J. Cell Biol. 127(2): 453-465
    • (1994) J. Cell Biol. , vol.127 , Issue.2 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 46
    • 0030878997 scopus 로고    scopus 로고
    • Gelsolin binding to phosphatidylinositol 4,5-bisphosphate is modulated by calcium and pH
    • Lin K. M., Wenegieme E., Lu P. J., Chen C. S. and Yin H. L. (1997) Gelsolin binding to phosphatidylinositol 4,5-bisphosphate is modulated by calcium and pH. J. Biol. Chem. 272(33): 20443-20450
    • (1997) J. Biol. Chem. , vol.272 , Issue.33 , pp. 20443-20450
    • Lin, K.M.1    Wenegieme, E.2    Lu, P.J.3    Chen, C.S.4    Yin, H.L.5
  • 47
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Yu F. X., Johnston P. A., Sudhof T. C. and Yin H. L. (1990) gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein. Science 250(4986): 1413-1415
    • (1990) Science , vol.250 , Issue.4986 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4
  • 49
    • 0042817834 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place
    • Doughman R. L., Firestone A. J. and Anderson R. A. (2003) Phosphatidylinositol phosphate kinases put PI4,5P(2) in its place. J. Membr. Biol. 194(2): 77-89
    • (2003) J. Membr. Biol. , vol.194 , Issue.2 , pp. 77-89
    • Doughman, R.L.1    Firestone, A.J.2    Anderson, R.A.3
  • 50
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin H. L. and Janmey P. A. (2003) Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65: 761-789
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 51
  • 52
    • 10344222932 scopus 로고    scopus 로고
    • A novel actin barbed-endcapping activity in EPS-8 regulates apical morphogenesis in intestinal cells of Caenorhabditis elegans
    • Croce A., Cassata G., Disanza A., Gagliani M. C., Tacchetti C., Malabarba M. G. et al. (2004) A novel actin barbed-endcapping activity in EPS-8 regulates apical morphogenesis in intestinal cells of Caenorhabditis elegans. Nat. Cell Biol. 6(12): 1173-1179
    • (2004) Nat. Cell Biol. , vol.6 , Issue.12 , pp. 1173-1179
    • Croce, A.1    Cassata, G.2    Disanza, A.3    Gagliani, M.C.4    Tacchetti, C.5    Malabarba, M.G.6
  • 54
    • 0347360339 scopus 로고    scopus 로고
    • The eps8 family of proteins links growth factor stimulation to actin reorganization generating functional redundancy in the Ras/Rac pathway
    • Offenhauser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I., Iannolo G. et al. (2004) The eps8 family of proteins links growth factor stimulation to actin reorganization generating functional redundancy in the Ras/Rac pathway. Mol. Biol. Cell 15(1): 91-98
    • (2004) Mol. Biol. Cell , vol.15 , Issue.1 , pp. 91-98
    • Offenhauser, N.1    Borgonovo, A.2    Disanza, A.3    Romano, P.4    Ponzanelli, I.5    Iannolo, G.6
  • 55
    • 0037294987 scopus 로고    scopus 로고
    • In silico analysis of the EPS8 gene family: Genomic organization, expression profile and protein structure
    • Tocchetti A., Confalonieri S., Scita G., Di Fiore P. P. and Betsholtz C. (2003) In silico analysis of the EPS8 gene family: genomic organization, expression profile and protein structure. Genomics 81(2): 234-244
    • (2003) Genomics , vol.81 , Issue.2 , pp. 234-244
    • Tocchetti, A.1    Confalonieri, S.2    Scita, G.3    Di Fiore, P.P.4    Betsholtz, C.5
  • 57
  • 58
    • 0035802118 scopus 로고    scopus 로고
    • An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine
    • Scita G., Tenca P., Areces L. B., Tocchetti A., Frittoli E., Giardina G. et al. (2001) An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine. J. Cell Biol. 154(5): 1031-144
    • (2001) J. Cell Biol. , vol.154 , Issue.5 , pp. 1031-1144
    • Scita, G.1    Tenca, P.2    Areces, L.B.3    Tocchetti, A.4    Frittoli, E.5    Giardina, G.6
  • 59
  • 60
    • 1842562381 scopus 로고    scopus 로고
    • Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation
    • Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G., Wehland J. et al. (2004) Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation. EMBO J. 23(4): 749-759
    • (2004) EMBO J. , vol.23 , Issue.4 , pp. 749-759
    • Steffen, A.1    Rottner, K.2    Ehinger, J.3    Innocenti, M.4    Scita, G.5    Wehland, J.6
  • 61
    • 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(7): 385-391
    • (2000) Nat. Cell Biol. , vol.2 , Issue.7 , pp. 385-391
    • Pantaloni, D.1    Boujemaa, R.2    Didry, D.3    Gounon, P.4    Carlier, M.F.5
  • 62
    • 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(5): 1009-1026
    • (1999) J. Cell Biol. , vol.145 , Issue.5 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 63
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • Zigmond S. H. (2004) Formin-induced nucleation of actin filaments. Curr. Opin. Cell Biol. 16(1): 99-105
    • (2004) Curr. Opin. Cell Biol. , vol.16 , Issue.1 , pp. 99-105
    • Zigmond, S.H.1
  • 64
    • 1642361261 scopus 로고    scopus 로고
    • Actin polymerization-driven molecular movement of mDia1 in living cells
    • Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J., Andou Y. et al. (2004) Actin polymerization-driven molecular movement of mDia1 in living cells. Science 303(5666): 2007-2010
    • (2004) Science , vol.303 , Issue.5666 , pp. 2007-2010
    • Higashida, C.1    Miyoshi, T.2    Fujita, A.3    Oceguera-Yanez, F.4    Monypenny, J.5    Andou, Y.6
  • 65
    • 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(Pt 13): 2603-2611
    • (2003) J. Cell Sci. , vol.116 , Issue.13 PART , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 66
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs H. N. and Pollard T. D. (1999) Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J. Biol. Chem. 274(46): 32531-32534
    • (1999) J. Biol. Chem. , vol.274 , Issue.46 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 67
    • 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. B. and Pollard T. D. (2000) Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404(6781): 1007-1011
    • (2000) Nature , vol.404 , Issue.6781 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.B.5    Pollard, T.D.6
  • 68
    • 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(11): 6181-6186
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.11 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 70
    • 0034983715 scopus 로고    scopus 로고
    • WASP and WAVE family proteins: Key molecules for rapid rearrangement of cortical actin filaments and cell movement
    • Takenawa T. and Miki H. (2001) WASP and WAVE family proteins: key molecules for rapid rearrangement of cortical actin filaments and cell movement. J. Cell Sci. 114(Pt 10): 1801-1809
    • (2001) J. Cell Sci. , vol.114 , Issue.10 PART , pp. 1801-1809
    • Takenawa, T.1    Miki, H.2
  • 71
    • 0032481290 scopus 로고    scopus 로고
    • Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization
    • Miki H. and Takenawa T. (1998) Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization. Biochem. Biophys. Res. Commun. 243(1): 73-78
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , Issue.1 , pp. 73-78
    • Miki, H.1    Takenawa, T.2
  • 72
    • 0041989754 scopus 로고    scopus 로고
    • A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
    • Panchal S. C., Kaiser D. A., Torres E., Pollard T. D. and Rosen M. K. (2003) A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nat. Struct. Biol. 10(8): 591-598
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.8 , pp. 591-598
    • Panchal, S.C.1    Kaiser, D.A.2    Torres, E.3    Pollard, T.D.4    Rosen, M.K.5
  • 73
    • 0035146636 scopus 로고    scopus 로고
    • Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
    • Marchand J. B., Kaiser D. A., Pollard T. D. and Higgs H. N. (2001) Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nat. Cell Biol. 3(1): 76-82
    • (2001) Nat. Cell Biol. , vol.3 , Issue.1 , pp. 76-82
    • Marchand, J.B.1    Kaiser, D.A.2    Pollard, T.D.3    Higgs, H.N.4
  • 74
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim A. S., Kakalis L. T., Abdul-Manan N., Liu G. A. and Rosen M. K. (2000) Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404(6774): 151-158
    • (2000) Nature , vol.404 , Issue.6774 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 75
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L. M. and Insall R. H. (1998) Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8(25): 1347-1356
    • (1998) Curr. Biol. , vol.8 , Issue.25 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 76
    • 0035094485 scopus 로고    scopus 로고
    • The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
    • Amann K. J. and Pollard T. D. (2001) The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat. Cell Biol. 3(3): 306-310
    • (2001) Nat. Cell Biol. , vol.3 , Issue.3 , pp. 306-310
    • Amann, K.J.1    Pollard, T.D.2
  • 77
    • 0035949529 scopus 로고    scopus 로고
    • Listeria protein ActA mimics WASp family proteins: It activates filament barbed end branching by Arp2/3 complex
    • Boujemaa-Paterski R., Gouin E., Hansen G., Samarin S., Le Clainche C., Didry D. et al. (2001) Listeria protein ActA mimics WASp family proteins: it activates filament barbed end branching by Arp2/3 complex. Biochemistry 40(38): 11390-11404
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11390-11404
    • Boujemaa-Paterski, R.1    Gouin, E.2    Hansen, G.3    Samarin, S.4    Le Clainche, C.5    Didry, D.6
  • 78
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
    • Svitkina T. M., Verkhovsky A. B., McQuade K. M. and Borisy G. G. (1997) Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J. Cell Biol. 139(2): 397-415
    • (1997) J. Cell Biol. , vol.139 , Issue.2 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 79
    • 0036558286 scopus 로고    scopus 로고
    • Visualisation of the actin cytoskeleton by cryo-electron microscopy
    • Resch G. P., Goldie K. N., Krebs A., Hoenger A. and Small J. V. (2002) Visualisation of the actin cytoskeleton by cryo-electron microscopy. J. Cell Sci. 115(Pt 9): 1877-1882
    • (2002) J. Cell Sci. , vol.115 , Issue.9 PART , pp. 1877-1882
    • Resch, G.P.1    Goldie, K.N.2    Krebs, A.3    Hoenger, A.4    Small, J.V.5
  • 81
    • 0038313144 scopus 로고    scopus 로고
    • ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays
    • Le Clainche C., Pantaloni D. and Carlier M. F. (2003) ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays. Proc. Natl. Acad. Sci. USA 100(11): 6337-6342
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.11 , pp. 6337-6342
    • Le Clainche, C.1    Pantaloni, D.2    Carlier, M.F.3
  • 82
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M., Pruyne D., Amberg D. C., Boone C. and Bretscher A. (2002) Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4(3): 260-269
    • (2002) Nat. Cell Biol. , vol.4 , Issue.3 , pp. 260-269
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 83
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista M., Blundell K., Longtine M. S., Chow C. J., Adames N., Pringle J. R. et al. (1997) Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276(5309): 118-122
    • (1997) Science , vol.276 , Issue.5309 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.S.3    Chow, C.J.4    Adames, N.5    Pringle, J.R.6
  • 84
    • 0037026486 scopus 로고    scopus 로고
    • Actin dynamics in the contractile ring during cytokinesis in fission yeast
    • Pelham R. J. and Chang F. (2002) Actin dynamics in the contractile ring during cytokinesis in fission yeast. Nature 419(6902): 82-86
    • (2002) Nature , vol.419 , Issue.6902 , pp. 82-86
    • Pelham, R.J.1    Chang, F.2
  • 85
    • 1342310742 scopus 로고    scopus 로고
    • Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables
    • Kobielak A., Pasolli H. A. and Fuchs E. (2004) Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat. Cell Biol. 6(1): 21-30
    • (2004) Nat. Cell Biol. , vol.6 , Issue.1 , pp. 21-30
    • Kobielak, A.1    Pasolli, H.A.2    Fuchs, E.3
  • 86
    • 0038325646 scopus 로고    scopus 로고
    • The formin-homology-domain-containing protein FHOD1 enhances cell migration
    • Koka S., Neudauer C. L., Li X., Lewis R. E., McCarthy J. B. and Westendorf J. J. (2003) The formin-homology-domain-containing protein FHOD1 enhances cell migration. J. Cell Sci. 116(Pt 9): 1745-1755
    • (2003) J. Cell Sci. , vol.116 , Issue.9 PART , pp. 1745-1755
    • Koka, S.1    Neudauer, C.L.2    Li, X.3    Lewis, R.E.4    McCarthy, J.B.5    Westendorf, J.J.6
  • 87
    • 0030911424 scopus 로고    scopus 로고
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A. et al. (1997) p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16(11): 3044-3056
    • (1997) EMBO J. , vol.16 , Issue.11 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6
  • 88
    • 0037382160 scopus 로고    scopus 로고
    • Disruption of the diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42
    • Peng J., Wallar B. J., Flanders A., Swiatek P. J. and Alberts A. S. (2003) Disruption of the diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr, Biol, 13(7): 534-545
    • (2003) Curr. Biol. , vol.13 , Issue.7 , pp. 534-545
    • Peng, J.1    Wallar, B.J.2    Flanders, A.3    Swiatek, P.J.4    Alberts, A.S.5
  • 89
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar B. J. and Alberts A. S. (2003) The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13(8): 435-446
    • (2003) Trends Cell Biol. , vol.13 , Issue.8 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 90
    • 0037458002 scopus 로고    scopus 로고
    • Mechanism of formin-induced nucleation of actin filaments
    • Pring M., Evangelista M., Boone C., Yang C. and Zigmond S. H. (2003) Mechanism of formin-induced nucleation of actin filaments. Biochemistry 42(2): 486-496
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 486-496
    • Pring, M.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Zigmond, S.H.5
  • 91
    • 0036049615 scopus 로고    scopus 로고
    • An actin nucleation mechanism mediated by Bni1 and profilin
    • Sagot I., Rodal A. A., Moseley J., Goode B. L. and Pellman D. (2002) An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 4(8): 626-631
    • (2002) Nat. Cell Biol. , vol.4 , Issue.8 , pp. 626-631
    • Sagot, I.1    Rodal, A.A.2    Moseley, J.3    Goode, B.L.4    Pellman, D.5
  • 92
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • Pruyne D., Evangelista M., Yang C., Bi E., Zigmond S., Bretscher A. et al. (2002) Role of formins in actin assembly: nucleation and barbed-end association. Science 297(5581): 612-615
    • (2002) Science , vol.297 , Issue.5581 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5    Bretscher, A.6
  • 93
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • in press
    • Romero S., Le Clainche C., Didry D., Egile C., Pantaloni D. and Carlier M. F. (2004) Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell, in press
    • (2004) Cell
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 94
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge K. and Wennerberg K. (2004) Rho and Rac take center stage. Cell 116(2): 167-179
    • (2004) Cell , vol.116 , Issue.2 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 95
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou M. and Hall A. (2004) Cell migration: Rho GTPases lead the way. Dev. Biol. 265(1): 23-32
    • (2004) Dev. Biol. , vol.265 , Issue.1 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 96
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley A. J. (2001) Rho GTPases and cell migration. J. Cell Sci. 114(Pt 15): 2713-2722
    • (2001) J. Cell Sci. , vol.114 , Issue.15 PART , pp. 2713-2722
    • Ridley, A.J.1
  • 97
    • 0942268723 scopus 로고    scopus 로고
    • Rho GTPases have diverse effects on the organization of the actin filament system
    • Aspenstrom P., Fransson A. and Saras J. (2004) Rho GTPases have diverse effects on the organization of the actin filament system. Biochem. J. 377(Pt 2): 327-337
    • (2004) Biochem. J. , vol.377 , Issue.2 PART , pp. 327-337
    • Aspenstrom, P.1    Fransson, A.2    Saras, J.3
  • 98
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A. and Hall A. (2002) Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16(13): 1587-1609
    • (2002) Genes Dev. , vol.16 , Issue.13 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 99
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A. J., Paterson H. F., Johnston C. L., Diekmann D. and Hall A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70(3): 401-410
    • (1992) Cell , vol.70 , Issue.3 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 100
    • 0035869649 scopus 로고    scopus 로고
    • Mechanisms of platelet-derived growth factor-induced chemotaxis
    • Ronnstrand L. and Heldin C. H. (2001) Mechanisms of platelet-derived growth factor-induced chemotaxis. Int. J. Cancer 91(6): 757-762
    • (2001) Int. J. Cancer , vol.91 , Issue.6 , pp. 757-762
    • Ronnstrand, L.1    Heldin, C.H.2
  • 101
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. (2000) Cell signaling by receptor tyrosine kinases. Cell 103(2): 211-225
    • (2000) Cell , vol.103 , Issue.2 , pp. 211-225
    • Schlessinger, J.1
  • 102
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon M. A. and Schlessinger J. (1994) Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem. Sci. 19(11): 459-463
    • (1994) Trends Biochem. Sci. , vol.19 , Issue.11 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 104
    • 0028429961 scopus 로고
    • Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling
    • Wennstrom S., Hawkins P., Cooke F. Hara K., Yonezawa K., Kasuga M. et al. (1994) Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling. Curr. Biol. 4(5): 385-393
    • (1994) Curr. Biol. , vol.4 , Issue.5 , pp. 385-393
    • Wennstrom, S.1    Hawkins, P.2    Cooke, F.3    Hara, K.4    Yonezawa, K.5    Kasuga, M.6
  • 105
    • 0025042770 scopus 로고
    • Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase
    • Kazlauskas A. and Cooper J. A. (1990) Phosphorylation of the PDGF receptor beta subunit creates a tight binding site for phosphatidylinositol 3 kinase. EMBO J. 9(10): 3279-3286
    • (1990) EMBO J. , vol.9 , Issue.10 , pp. 3279-3286
    • Kazlauskas, A.1    Cooper, J.A.2
  • 106
    • 0027217074 scopus 로고
    • Ash/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGF
    • Matuoka K., Shibasaki F., Shibata M. and Takenawa T. (1993) Ash/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGF. EMBO J. 12(9): 3467-3473
    • (1993) EMBO J. , vol.12 , Issue.9 , pp. 3467-3473
    • Matuoka, K.1    Shibasaki, F.2    Shibata, M.3    Takenawa, T.4
  • 107
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday L. and Downward J. (1993) Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73(3): 611-620
    • (1993) Cell , vol.73 , Issue.3 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 108
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein E. J., Daly R. J., Batzer A. G., Li W., Margolis B., Lammers R. et al. (1992) The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 70(3): 431-442
    • (1992) Cell , vol.70 , Issue.3 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3    Li, W.4    Margolis, B.5    Lammers, R.6
  • 109
    • 0036308458 scopus 로고    scopus 로고
    • Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils
    • Wang F., Herzmark P., Weiner O. D., Srinivasan S., Servant G. and Bourne H. R. (2002) Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils. Nat. Cell Biol. 4(7): 513-518
    • (2002) Nat. Cell Biol. , vol.4 , Issue.7 , pp. 513-518
    • Wang, F.1    Herzmark, P.2    Weiner, O.D.3    Srinivasan, S.4    Servant, G.5    Bourne, H.R.6
  • 110
    • 2342552557 scopus 로고    scopus 로고
    • PtdIns(3,4,5)P3 binding is necessary for WAVE2-induced formation of lamellipodia
    • Oikawa T., Yamaguchi H., Itoh T., Kato M., Ijuin T., Yamazaki D. et al. (2004) PtdIns(3,4,5)P3 binding is necessary for WAVE2-induced formation of lamellipodia. Nat. Cell Biol. 6(5): 420-426
    • (2004) Nat. Cell Biol. , vol.6 , Issue.5 , pp. 420-426
    • Oikawa, T.1    Yamaguchi, H.2    Itoh, T.3    Kato, M.4    Ijuin, T.5    Yamazaki, D.6
  • 111
    • 0034921007 scopus 로고    scopus 로고
    • Tumor suppressor PTEN: Modulator of cell signaling, growth, migration and apoptosis
    • Yamada K. M. and Araki M. (2001) Tumor suppressor PTEN: modulator of cell signaling, growth, migration and apoptosis. J. Cell Sci. 114(Pt 13): 2375-2382
    • (2001) J. Cell Sci. , vol.114 , Issue.13 PART , pp. 2375-2382
    • Yamada, K.M.1    Araki, M.2
  • 112
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • Lee J. O., Yang H., Georgescu M. M., Di Cristofano A., Maehama T., Shi Y. et al. (1999) Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99(3): 323-334
    • (1999) Cell , vol.99 , Issue.3 , pp. 323-334
    • Lee, J.O.1    Yang, H.2    Georgescu, M.M.3    Di Cristofano, A.4    Maehama, T.5    Shi, Y.6
  • 113
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T. and Dixon J. E. (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273(22): 13375-13378
    • (1998) J. Biol. Chem. , vol.273 , Issue.22 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 114
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • Merlot S. and Firtel R. A. (2003) Leading the way: directional sensing through phosphatidylinositol 3-kinase and other signaling pathways. J. Cell Sci. 116(Pt 17): 3471-3478
    • (2003) J. Cell Sci. , vol.116 , Issue.17 PART , pp. 3471-3478
    • Merlot, S.1    Firtel, R.A.2
  • 115
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes C. D., Hawkins P., Stephens L. and Hall A. (1995) Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J. Cell Sci. 108 (Pt 1): 225-233
    • (1995) J. Cell Sci. , vol.108 , Issue.1 PART , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 116
    • 0028947199 scopus 로고
    • Phosphoinositide 3-kinase as an upstream regulator of the small GTP-binding protein Rac in the insulin signaling of membrane ruffling
    • Kotani K., Hara K., Yonezawa K. and Kasuga M. (1995) Phosphoinositide 3-kinase as an upstream regulator of the small GTP-binding protein Rac in the insulin signaling of membrane ruffling. Biochem. Biophys. Res. Commun. 208(3): 985-990
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , Issue.3 , pp. 985-990
    • Kotani, K.1    Hara, K.2    Yonezawa, K.3    Kasuga, M.4
  • 117
    • 0029278739 scopus 로고
    • PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase
    • Hawkins P. T., Eguinoa A., Qiu R. G., Stokoe D., Cooke F. T., Walters R. et al. (1995) PDGF stimulates an increase in GTP-Rac via activation of phosphoinositide 3-kinase. Curr. Biol. 5(4): 393-403
    • (1995) Curr. Biol. , vol.5 , Issue.4 , pp. 393-403
    • Hawkins, P.T.1    Eguinoa, A.2    Qiu, R.G.3    Stokoe, D.4    Cooke, F.T.5    Walters, R.6
  • 118
    • 0038538430 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-dependent activation of Rac
    • Welch H. C., Coadwell W. J., Stephens L. R. and Hawkins P. T. (2003) Phosphoinositide 3-kinase-dependent activation of Rac. FEBS Lett. 546(1): 93-97
    • (2003) FEBS Lett. , vol.546 , Issue.1 , pp. 93-97
    • Welch, H.C.1    Coadwell, W.J.2    Stephens, L.R.3    Hawkins, P.T.4
  • 119
    • 0037129193 scopus 로고    scopus 로고
    • SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling of membrane ruffling
    • Shinohara M., Terada Y., Iwamatsu A., Shinohara A., Mochizuki N., Higuchi M. et al. (2002) SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling of membrane ruffling. Nature 416(6882): 759-763
    • (2002) Nature , vol.416 , Issue.6882 , pp. 759-763
    • Shinohara, M.1    Terada, Y.2    Iwamatsu, A.3    Shinohara, A.4    Mochizuki, N.5    Higuchi, M.6
  • 121
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo X. R. (2000) Regulatory and signaling properties of the Vav family. Mol. Cell. Biol. 20(5): 1461-1477
    • (2000) Mol. Cell. Biol. , vol.20 , Issue.5 , pp. 1461-1477
    • Bustelo, X.R.1
  • 122
    • 0037115488 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
    • Cote J. F. and Vuori K. (2002) Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J. Cell Sci. 115(Pt 24): 4901-4913
    • (2002) J. Cell Sci. , vol.115 , Issue.24 PART , pp. 4901-4913
    • Cote, J.F.1    Vuori, K.2
  • 125
    • 0036531884 scopus 로고    scopus 로고
    • How signaling proteins integrate multiple inputs: A comparison of N-WASP and Cdk2
    • Prehoda K. E. and Lim W. A. (2002) How signaling proteins integrate multiple inputs: a comparison of N-WASP and Cdk2. Curr. Opin. Cell Biol. 14(2): 149-154
    • (2002) Curr. Opin. Cell Biol. , vol.14 , Issue.2 , pp. 149-154
    • Prehoda, K.E.1    Lim, W.A.2
  • 126
    • 0032403083 scopus 로고    scopus 로고
    • WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac
    • Miki H., Suetsugu S. and Takenawa T. (1998) WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J. 17(23): 6932-6941
    • (1998) EMBO J. , vol.17 , Issue.23 , pp. 6932-6941
    • Miki, H.1    Suetsugu, S.2    Takenawa, T.3
  • 127
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda K. E., Scott J. A., Mullins R. D. and Lim W. A. (2000) Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290(5492): 801-806
    • (2000) Science , vol.290 , Issue.5492 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 128
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R., Ho H. Y. and Kirschner M. W. (2000) Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J. Cell Biol. 150(6): 1299-1310
    • (2000) J. Cell Biol. , vol.150 , Issue.6 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 129
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T. et al. (1999) The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97(2): 221-231
    • (1999) Cell , vol.97 , Issue.2 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6
  • 131
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S. and Takenawa T. (2000) IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408(6813): 732-735
    • (2000) Nature , vol.408 , Issue.6813 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 132
    • 2442458996 scopus 로고    scopus 로고
    • A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein
    • Yamagishi A., Masuda M., Ohki T., Onishi H. and Mochizuki N. (2004) A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J. Biol. Chem. 279(15): 14929-14936
    • (2004) J. Biol. Chem. , vol.279 , Issue.15 , pp. 14929-14936
    • Yamagishi, A.1    Masuda, M.2    Ohki, T.3    Onishi, H.4    Mochizuki, N.5
  • 133
    • 0035809181 scopus 로고    scopus 로고
    • Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin
    • Govind S., Kozma R., Monfries C., Lim L. and Ahmed S. (2001) Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin. J. Cell Biol. 152(3): 579-594
    • (2001) J. Cell Biol. , vol.152 , Issue.3 , pp. 579-594
    • Govind, S.1    Kozma, R.2    Monfries, C.3    Lim, L.4    Ahmed, S.5
  • 134
  • 135
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S., Rohatgi R., Podtelejnikov A. V., Mann M. and Kirschner M. W. (2002) Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418(6899): 790-793
    • (2002) Nature , vol.418 , Issue.6899 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 138
    • 0031972690 scopus 로고    scopus 로고
    • p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase
    • Kobayashi K., Kuroda S., Fukata M., Nakamura T., Nagase T., Nomura N. et al. (1998) p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase. J. Biol. Chem. 273(1): 291-295
    • (1998) J. Biol. Chem. , vol.273 , Issue.1 , pp. 291-295
    • Kobayashi, K.1    Kuroda, S.2    Fukata, M.3    Nakamura, T.4    Nagase, T.5    Nomura, N.6
  • 139
    • 0035896436 scopus 로고    scopus 로고
    • Scar/WAVE is localised at the tips of protruding lamellipodia in living cells
    • Hahne P., Sechi A., Benesch S. and Small J. V. (2001) Scar/WAVE is localised at the tips of protruding lamellipodia in living cells. FEBS Lett. 492(3): 215-220
    • (2001) FEBS Lett. , vol.492 , Issue.3 , pp. 215-220
    • Hahne, P.1    Sechi, A.2    Benesch, S.3    Small, J.V.4
  • 140
    • 0242286595 scopus 로고    scopus 로고
    • Abi, Sra1 and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions
    • Kunda P., Craig G., Dominguez V. and Baum B. (2003) Abi, Sra1 and Kette control the stability and localization of SCAR/WAVE to regulate the formation of actin-based protrusions. Curr. Biol. 13(21): 1867-1875
    • (2003) Curr. Biol. , vol.13 , Issue.21 , pp. 1867-1875
    • Kunda, P.1    Craig, G.2    Dominguez, V.3    Baum, B.4
  • 141
    • 4644303503 scopus 로고    scopus 로고
    • Interchangeable functions of Arabidopsis PIROGI and the human WAVE complex subunit SRA1 during leaf epidermal development
    • Basu D., El-Assal Sel D., Le J., Mallery E. L. and Szymanski D. B. (2004) Interchangeable functions of Arabidopsis PIROGI and the human WAVE complex subunit SRA1 during leaf epidermal development. Development 131(17): 4345-4355
    • (2004) Development , vol.131 , Issue.17 , pp. 4345-4355
    • Basu, D.1    El-Assal Sel, D.2    Le, J.3    Mallery, E.L.4    Szymanski, D.B.5
  • 142
    • 4544267439 scopus 로고    scopus 로고
    • NAPP and PIRP encode subunits of a putative wave regulatory protein complex involved in plant cell morphogenesis
    • Brembu T., Winge P., Seem M. and Bones A. M. (2004) NAPP and PIRP encode subunits of a putative wave regulatory protein complex involved in plant cell morphogenesis. Plant Cell 16(9): 2335-2349
    • (2004) Plant Cell , vol.16 , Issue.9 , pp. 2335-2349
    • Brembu, T.1    Winge, P.2    Seem, M.3    Bones, A.M.4
  • 143
    • 4143149709 scopus 로고    scopus 로고
    • Arabidopsis GNARLED encodes a NAP125 homolog that positively regulates ARP2/3
    • El-Assal Sel D., Le J., Basu D., Mallery E. L. and Szymanski D. B. (2004) Arabidopsis GNARLED encodes a NAP125 homolog that positively regulates ARP2/3. Curr. Biol. 14(15): 1405-1409
    • (2004) Curr. Biol. , vol.14 , Issue.15 , pp. 1405-1409
    • El-Assal Sel, D.1    Le, J.2    Basu, D.3    Mallery, E.L.4    Szymanski, D.B.5
  • 144
    • 8644267397 scopus 로고    scopus 로고
    • The Arabidopsis GNARLED gene encodes the NAP125 homolog and controls several actin-based cell shape changes
    • Zimmermann I., Saedler R., Mutondo M. and Hulskamp M. (2004) The Arabidopsis GNARLED gene encodes the NAP125 homolog and controls several actin-based cell shape changes. Mol. Genet. Genomics
    • (2004) Mol. Genet. Genomics
    • Zimmermann, I.1    Saedler, R.2    Mutondo, M.3    Hulskamp, M.4
  • 145
    • 0042921214 scopus 로고    scopus 로고
    • PIR121 regulates pseudopod dynamics and SCAR activity in Dictyosfelium
    • Blagg S. L., Stewart M., Sambles C. and Insall R. H. (2003) PIR121 regulates pseudopod dynamics and SCAR activity in Dictyosfelium. Curr. Biol. 13(17): 1480-1487
    • (2003) Curr. Biol. , vol.13 , Issue.17 , pp. 1480-1487
    • Blagg, S.L.1    Stewart, M.2    Sambles, C.3    Insall, R.H.4
  • 146
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards D. C., Sanders L. C., Bokoch G. M. and Gill G. N. (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat. Cell Biol. 1(5): 253-259
    • (1999) Nat. Cell Biol. , vol.1 , Issue.5 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 147
    • 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. et al. (1998) Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393(6687): 809-812
    • (1998) Nature , vol.393 , Issue.6687 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6
  • 148
    • 0035153556 scopus 로고    scopus 로고
    • Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis
    • Chen J., Godt D., Gunsalus K., Kiss I., Goldberg M. and Laski F. A. (2001) Cofilin/ADF is required for cell motility during Drosophila ovary development and oogenesis. Nat. Cell Biol. 3(2): 204-209
    • (2001) Nat. Cell Biol. , vol.3 , Issue.2 , pp. 204-209
    • Chen, J.1    Godt, D.2    Gunsalus, K.3    Kiss, I.4    Goldberg, M.5    Laski, F.A.6
  • 149
    • 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(5): 1119-1128
    • (2000) J. Cell Biol. , vol.151 , Issue.5 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 150
    • 0033198879 scopus 로고    scopus 로고
    • Putting a new twist on actin: ADF/cofilins modulate actin dynamics
    • Bamburg J. R., McGough A. and Ono S. (1999) Putting a new twist on actin: ADF/cofilins modulate actin dynamics. Trends Cell Biol. 9(9): 364-370
    • (1999) Trends Cell Biol. , vol.9 , Issue.9 , pp. 364-370
    • Bamburg, J.R.1    McGough, A.2    Ono, S.3
  • 151
    • 0034628109 scopus 로고    scopus 로고
    • Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly
    • Tolias K. F., Hartwig J. H., Ishihara H., Shibasaki Y., Cantley L. C. and Carpenter C. L. (2000) Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly. Curr. Biol. 10(3): 153-156
    • (2000) Curr. Biol. , vol.10 , Issue.3 , pp. 153-156
    • Tolias, K.F.1    Hartwig, J.H.2    Ishihara, H.3    Shibasaki, Y.4    Cantley, L.C.5    Carpenter, C.L.6
  • 152
    • 0034597599 scopus 로고    scopus 로고
    • Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis
    • Malecz N., McCabe P. C., Spaargaren C., Qiu R., Chuang Y. and Symons M. (2000) Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis. Curr. Biol. 10(21): 1383-1386
    • (2000) Curr. Biol. , vol.10 , Issue.21 , pp. 1383-1386
    • Malecz, N.1    McCabe, P.C.2    Spaargaren, C.3    Qiu, R.4    Chuang, Y.5    Symons, M.6
  • 154
    • 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(47): 33179-33182
    • (1999) J. Biol. Chem. , vol.274 , Issue.47 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 155
    • 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(5): 1362-1370
    • (1998) EMBO J. , vol.17 , Issue.5 , pp. 1362-1370
    • Azuma, T.1    Witke, W.2    Stossel, T.P.3    Hartwig, J.H.4    Kwiatkowski, D.J.5
  • 156
    • 0031974716 scopus 로고    scopus 로고
    • The small GTP-binding protein Rac promotes the dissociation of gelsolin from actin filaments in neutrophils
    • Arcaro A. (1998) The small GTP-binding protein Rac promotes the dissociation of gelsolin from actin filaments in neutrophils. J. Biol. Chem. 273(2): 805-813
    • (1998) J. Biol. Chem. , vol.273 , Issue.2 , pp. 805-813
    • Arcaro, A.1
  • 157
    • 0035921434 scopus 로고    scopus 로고
    • Comparisons of CapG and gelsolin-null macrophages: Demonstration of a unique role for CapG in receptor-mediated ruffling, phagocytosis, and vesicle rocketing
    • Witke W., Li W., Kwiatkowski D. J. and Southwick F. S. (2001) Comparisons of CapG and gelsolin-null macrophages: demonstration of a unique role for CapG in receptor-mediated ruffling, phagocytosis, and vesicle rocketing. J. Cell Biol. 154(4): 775-784
    • (2001) J. Cell Biol. , vol.154 , Issue.4 , pp. 775-784
    • Witke, W.1    Li, W.2    Kwiatkowski, D.J.3    Southwick, F.S.4
  • 158
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke W., Sharpe A. H., Hartwig J. H., Azuma T., Stossel T. P. and Kwiatkowski D. J. (1995) Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell 81(1): 41-51
    • (1995) Cell , vol.81 , Issue.1 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 160
    • 0032559211 scopus 로고    scopus 로고
    • Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos
    • Nimnual A. S., Yatsula B. A. and Bar-Sagi D. (1998) Coupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos. Science 279(5350): 560-563
    • (1998) Science , vol.279 , Issue.5350 , pp. 560-563
    • Nimnual, A.S.1    Yatsula, B.A.2    Bar-Sagi, D.3
  • 161
    • 0036293357 scopus 로고    scopus 로고
    • WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac
    • Miki H. and Takenawa T. (2002) WAVE2 serves a functional partner of IRSp53 by regulating its interaction with Rac. Biochem. Biophys. Res. Commun. 293(1): 93-99
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , Issue.1 , pp. 93-99
    • Miki, H.1    Takenawa, T.2


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