메뉴 건너뛰기




Volumn 133, Issue 5, 2008, Pages 841-851

Capping Protein Increases the Rate of Actin-Based Motility by Promoting Filament Nucleation by the Arp2/3 Complex

Author keywords

CELLBIO

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX;

EID: 43949143882     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.04.011     Document Type: Article
Times cited : (202)

References (44)
  • 2
    • 18044379419 scopus 로고    scopus 로고
    • Actin nucleation: spire - actin nucleator in a class of its own
    • B. Baum P. Kunda Actin nucleation: spire - actin nucleator in a class of its own Curr. Biol. 15 2005 R305 R308
    • (2005) Curr. Biol. , vol.15 , pp. R305-R308
    • Baum, B.1    Kunda, P.2
  • 6
    • 2342505220 scopus 로고    scopus 로고
    • Biophysical parameters influence actin-based movement, trajectory, and initiation in a cell-free system
    • L.A. Cameron J.R. Robbins M.J. Footer J.A. Theriot Biophysical parameters influence actin-based movement, trajectory, and initiation in a cell-free system Mol. Biol. Cell 15 2004 2312 2323
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2312-2323
    • Cameron, L.A.1    Robbins, J.R.2    Footer, M.J.3    Theriot, J.A.4
  • 7
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • M.F. Carlier D. Pantaloni Control of actin dynamics in cell motility J. Mol. Biol. 269 1997 459 467
    • (1997) J. Mol. Biol. , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 8
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains
    • C. Co D.T. Wong S. Gierke V. Chang J. Taunton Mechanism of actin network attachment to moving membranes: barbed end capture by N-WASP WH2 domains Cell 128 2007 901 913
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 9
    • 0021984210 scopus 로고
    • Effect of capping protein on the kinetics of actin polymerization
    • J.A. Cooper T.D. Pollard Effect of capping protein on the kinetics of actin polymerization Biochemistry 24 1985 793 799
    • (1985) Biochemistry , vol.24 , pp. 793-799
    • Cooper, J.A.1    Pollard, T.D.2
  • 10
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly
    • G.A. Dabiri J.M. Sanger D.A. Portnoy F.S. Southwick Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly Proc. Natl. Acad. Sci. USA 87 1990 6068 6072
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 11
    • 19344373111 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2
    • M.J. Dayel R.D. Mullins Activation of Arp2/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2 PLoS Biol. 2 2004 E91
    • (2004) PLoS Biol. , vol.2 , pp. E91
    • Dayel, M.J.1    Mullins, R.D.2
  • 12
    • 0035910044 scopus 로고    scopus 로고
    • Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments
    • M.J. Dayel E.A. Holleran R.D. Mullins Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments Proc. Natl. Acad. Sci. USA 98 2001 14871 14876
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14871-14876
    • Dayel, M.J.1    Holleran, E.A.2    Mullins, R.D.3
  • 13
    • 0030728491 scopus 로고    scopus 로고
    • Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium
    • R.J. Eddy J. Han J.S. Condeelis Capping protein terminates but does not initiate chemoattractant-induced actin assembly in Dictyostelium J. Cell Biol. 139 1997 1243 1253
    • (1997) J. Cell Biol. , vol.139 , pp. 1243-1253
    • Eddy, R.J.1    Han, J.2    Condeelis, J.S.3
  • 14
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: an actin nucleator comes of age
    • E.D. Goley M.D. Welch The ARP2/3 complex: an actin nucleator comes of age Nat. Rev. Mol. Cell Biol. 7 2006 713 726
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 713-726
    • Goley, E.D.1    Welch, M.D.2
  • 15
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • E.D. Goley S.E. Rodenbusch A.C. Martin M.D. Welch Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor Mol. Cell 16 2004 269 279
    • (2004) Mol. Cell , vol.16 , pp. 269-279
    • Goley, E.D.1    Rodenbusch, S.E.2    Martin, A.C.3    Welch, M.D.4
  • 17
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • H.N. Higgs L. Blanchoin T.D. Pollard Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization Biochemistry 38 1999 15212 15222
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 19
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • J.H. Iwasa R.D. Mullins Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly Curr. Biol. 17 2007 395 406
    • (2007) Curr. Biol. , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 20
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • M. Kaksonen Y. Sun D.G. Drubin A pathway for association of receptors, adaptors, and actin during endocytic internalization Cell 115 2003 475 487
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 21
    • 0028786352 scopus 로고
    • Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba
    • J.F. Kelleher S.J. Atkinson T.D. Pollard Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba J. Cell Biol. 131 1995 385 397
    • (1995) J. Cell Biol. , vol.131 , pp. 385-397
    • Kelleher, J.F.1    Atkinson, S.J.2    Pollard, T.D.3
  • 22
    • 33744514937 scopus 로고    scopus 로고
    • Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex
    • A.E. Kelly H. Kranitz V. Dotsch R.D. Mullins Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex J. Biol. Chem. 281 2006 10589 10597
    • (2006) J. Biol. Chem. , vol.281 , pp. 10589-10597
    • Kelly, A.E.1    Kranitz, H.2    Dotsch, V.3    Mullins, R.D.4
  • 23
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • D.R. Kovar Molecular details of formin-mediated actin assembly Curr. Opin. Cell Biol. 18 2006 11 17
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 11-17
    • Kovar, D.R.1
  • 25
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • T.P. Loisel R. Boujemaa D. Pantaloni M.F. Carlier Reconstitution of actin-based motility of Listeria and Shigella using pure proteins Nature 401 1999 613 616
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 26
    • 0030670302 scopus 로고    scopus 로고
    • Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins
    • L.M. Machesky E. Reeves F. Wientjes F.J. Mattheyse A. Grogan N.F. Totty A.L. Burlingame J.J. Hsuan A.W. Segal Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins Biochem. J. 328 1997 105 112
    • (1997) Biochem. J. , vol.328 , pp. 105-112
    • Machesky, L.M.1    Reeves, E.2    Wientjes, F.3    Mattheyse, F.J.4    Grogan, A.5    Totty, N.F.6    Burlingame, A.L.7    Hsuan, J.J.8    Segal, A.W.9
  • 27
    • 0035146636 scopus 로고    scopus 로고
    • Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
    • J.B. Marchand D.A. Kaiser T.D. Pollard H.N. Higgs Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex Nat. Cell Biol. 3 2001 76 82
    • (2001) Nat. Cell Biol. , vol.3 , pp. 76-82
    • Marchand, J.B.1    Kaiser, D.A.2    Pollard, T.D.3    Higgs, H.N.4
  • 28
    • 33746646463 scopus 로고    scopus 로고
    • Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation
    • A.C. Martin M.D. Welch D.G. Drubin Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation Nat. Cell Biol. 8 2006 826 833
    • (2006) Nat. Cell Biol. , vol.8 , pp. 826-833
    • Martin, A.C.1    Welch, M.D.2    Drubin, D.G.3
  • 29
    • 0033790639 scopus 로고    scopus 로고
    • Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3
    • R.C. May E. Caron A. Hall L.M. Machesky Involvement of the Arp2/3 complex in phagocytosis mediated by FcgammaR or CR3 Nat. Cell Biol. 2 2000 246 248
    • (2000) Nat. Cell Biol. , vol.2 , pp. 246-248
    • May, R.C.1    Caron, E.2    Hall, A.3    Machesky, L.M.4
  • 30
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end
    • M.R. Mejillano S. Kojima D.A. Applewhite F.B. Gertler T.M. Svitkina G.G. Borisy Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end Cell 118 2004 363 373
    • (2004) Cell , vol.118 , 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
  • 31
    • 1842419430 scopus 로고    scopus 로고
    • Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts
    • C.J. Merrifield B. Qualmann M.M. Kessels W. Almers Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts Eur. J. Cell Biol. 83 2004 13 18
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 13-18
    • Merrifield, C.J.1    Qualmann, B.2    Kessels, M.M.3    Almers, W.4
  • 32
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing
    • T. Miyoshi T. Tsuji C. Higashida M. Hertzog A. Fujita S. Narumiya G. Scita N. Watanabe Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing J. Cell Biol. 175 2006 947 955
    • (2006) J. Cell Biol. , vol.175 , pp. 947-955
    • Miyoshi, T.1    Tsuji, T.2    Higashida, C.3    Hertzog, M.4    Fujita, A.5    Narumiya, S.6    Scita, G.7    Watanabe, N.8
  • 33
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • A. Mogilner G. Oster Cell motility driven by actin polymerization Biophys. J. 71 1996 3030 3045
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 34
    • 0033594548 scopus 로고    scopus 로고
    • Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts
    • R.D. Mullins T.D. Pollard Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts Curr. Biol. 9 1999 405 415
    • (1999) Curr. Biol. , vol.9 , pp. 405-415
    • Mullins, R.D.1    Pollard, T.D.2
  • 35
    • 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
    • R.D. Mullins J.A. Heuser T.D. Pollard 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 1998 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
  • 36
    • 4644298002 scopus 로고    scopus 로고
    • Actin filaments align into hollow comets for rapid VASP-mediated propulsion
    • J. Plastino S. Olivier C. Sykes Actin filaments align into hollow comets for rapid VASP-mediated propulsion Curr. Biol. 14 2004 1766 1771
    • (2004) Curr. Biol. , vol.14 , pp. 1766-1771
    • Plastino, J.1    Olivier, S.2    Sykes, C.3
  • 38
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides
    • D.A. Schafer P.B. Jennings J.A. Cooper Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides J. Cell Biol. 135 1996 169 179
    • (1996) J. Cell Biol. , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 42
    • 0030802671 scopus 로고    scopus 로고
    • The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly
    • M.D. Welch A.H. DePace S. Verma A. Iwamatsu T.J. Mitchison The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly J. Cell Biol. 138 1997 375 384
    • (1997) J. Cell Biol. , vol.138 , pp. 375-384
    • Welch, M.D.1    DePace, A.H.2    Verma, S.3    Iwamatsu, A.4    Mitchison, T.J.5
  • 44
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • D. Yarar W. To A. Abo M.D. Welch The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex Curr. Biol. 9 1999 555 558
    • (1999) Curr. Biol. , vol.9 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.