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Volumn 36, Issue , 2007, Pages 451-477

Regulation of actin filament assembly by Arp2/3 complex and formins

Author keywords

Cortactin; Profilin; Scar; WASp; WAVE

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; CORTACTIN; METHENAMINE; PROFILIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 34247644614     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.35.040405.101936     Document Type: Review
Times cited : (778)

References (135)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related form in homology protein autoregulatory domain
    • Alberts AS. 2001. Identification of a carboxyl-terminal diaphanous-related form in homology protein autoregulatory domain. J. Biol. Chem. 276:2824-30
    • (2001) J. Biol. Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 2
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection microscopy
    • Amann KJ, Pollard TD. 2001. Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection microscopy. Proc. Natl. Acad. Sci. USA 98:15009-13
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 3
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilins
    • Andrianantoandro E, Pollard TD. 2006. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilins. Mol. Cell 24:13-23
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 4
    • 33644939588 scopus 로고    scopus 로고
    • WTP: A multifunctional protein involved in actin cytoskeleton regulation
    • Anton IM, Jones GE. 2006. WTP: a multifunctional protein involved in actin cytoskeleton regulation. Eur. J. Cell Biol. 85:295-304
    • (2006) Eur. J. Cell Biol , vol.85 , pp. 295-304
    • Anton, I.M.1    Jones, G.E.2
  • 5
    • 33645528219 scopus 로고    scopus 로고
    • A role for cortactin in Listeria monocytogenes invasion of NIH 3T3 cells, but not in its intracellular motility
    • Barroso C, Rodenbusch SE, Welch MD, Drubin DG. 2006. A role for cortactin in Listeria monocytogenes invasion of NIH 3T3 cells, but not in its intracellular motility. Cell Motil. Cytoskelet. 63:231-43
    • (2006) Cell Motil. Cytoskelet , vol.63 , pp. 231-243
    • Barroso, C.1    Rodenbusch, S.E.2    Welch, M.D.3    Drubin, D.G.4
  • 7
    • 0742289599 scopus 로고    scopus 로고
    • Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species
    • Beltzner CC, Pollard TD. 2004. Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. J. Mol. Biol. 336:551-65
    • (2004) J. Mol. Biol , vol.336 , pp. 551-565
    • Beltzner, C.C.1    Pollard, T.D.2
  • 9
    • 0042921214 scopus 로고    scopus 로고
    • PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium
    • Blagg SL, Stewart M, Sambles C, Insall RH. 2003. PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium Curr. Biol. 13:1480-87
    • (2003) Curr. Biol , vol.13 , pp. 1480-1487
    • Blagg, S.L.1    Stewart, M.2    Sambles, C.3    Insall, R.H.4
  • 10
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASp/Scar proteins
    • Blanchoin L, Amann KJ, Higgs HN, Marchand JB, Kaiser DA, Pollard TD. 2000. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASp/Scar proteins. Nature 404:1007-11
    • (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
  • 11
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin L, Pollard TD. 1999. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274:15538-46
    • (1999) J. Biol. Chem , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 12
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of bound ATP by polymerized actin depends on the bound divalent cation but not profilin
    • Blanchoin L, Pollard TD. 2002. Hydrolysis of bound ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry 41:597-602
    • (2002) Biochemistry , vol.41 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 13
    • 0034687235 scopus 로고    scopus 로고
    • Interaction of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • Blanchoin L, Pollard TD, Mullins RD. 2000. Interaction of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr. Biol. 10:1273-82
    • (2000) Curr. Biol , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 16
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier MF, Laurent V, Santolini J, Melki R, Didry D, et al. 1997. Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136:1307-22
    • (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
  • 17
    • 0034698158 scopus 로고    scopus 로고
    • Grb2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich Syndrome protein (N-WASP) with actin-related-protein (Arp2/3) complex
    • Carlier MF, Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, et al. 2000. Grb2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich Syndrome protein (N-WASP) with actin-related-protein (Arp2/3) complex. J. Biol. Chem. 275:21946-52
    • (2000) J. Biol. Chem , vol.275 , pp. 21946-21952
    • Carlier, M.F.1    Nioche, P.2    Broutin-L'Hermite, I.3    Boujemaa, R.4    Le Clainche, C.5
  • 18
    • 0041885217 scopus 로고    scopus 로고
    • The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe
    • Carnahan RH, Gould KL. 2003. The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomyces pombe. J. Cell Biol. 162:851-62
    • (2003) J. Cell Biol , vol.162 , pp. 851-862
    • Carnahan, R.H.1    Gould, K.L.2
  • 19
    • 0030958087 scopus 로고    scopus 로고
    • cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang F, Drubin D, Nurse P. 1997. cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137:169-82
    • (1997) J. Cell Biol , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 20
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D, Kerff F, Graceffa P, Grabarek Z, Langsetmo K, Dominguez R. 2005. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 102:16644-49
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16644-16649
    • Chereau, D.1    Kerff, F.2    Graceffa, P.3    Grabarek, Z.4    Langsetmo, K.5    Dominguez, R.6
  • 21
    • 0035910044 scopus 로고    scopus 로고
    • Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments
    • Dayel MJ, Flolleran RD, Mullins DM. 2001. Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments. Proc. Natl. Acad. Sci. USA 98:14871-76
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14871-14876
    • Dayel, M.J.1    Flolleran, R.D.2    Mullins, D.M.3
  • 22
    • 19344373111 scopus 로고    scopus 로고
    • Dayel MJ, Mullins RD. 2004. 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(e91):476-85
    • Dayel MJ, Mullins RD. 2004. 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(e91):476-85
  • 24
    • 33645731661 scopus 로고    scopus 로고
    • BRICK1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabidopsis
    • Djakovic S, Dyachok J, Burke M, Frank MJ, Smith LG. 2006. BRICK1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabidopsis. Development 133:1091-100
    • (2006) Development , vol.133 , pp. 1091-1100
    • Djakovic, S.1    Dyachok, J.2    Burke, M.3    Frank, M.J.4    Smith, L.G.5
  • 25
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nek
    • Eden S, Rohatgi R, Podtelejnikov AV, Mann M, Kirschner MW. 2002. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nek. Nature 418:790-93
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 26
    • 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 TP, Laurent V, Li R, Pantaloni D, 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. 146:1319-32
    • (1999) J. Cell Biol , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5
  • 27
    • 27844455570 scopus 로고    scopus 로고
    • Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
    • Egile C, Rouiller I, Xu XP, Volkmann N, Li R, Hanein D. 2005. Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions. PLoS Biol. 3:1902-9
    • (2005) PLoS Biol , vol.3 , pp. 1902-1909
    • Egile, C.1    Rouiller, I.2    Xu, X.P.3    Volkmann, N.4    Li, R.5    Hanein, D.6
  • 28
    • 0036514271 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A. 2002. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4:32-41
    • (2002) Nat. Cell Biol , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 29
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach B, Chang F. 2001. Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11:1656-65
    • (2001) Curr. Biol , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 30
  • 31
    • 34547455419 scopus 로고    scopus 로고
    • Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy
    • In press
    • Fujiwara I, Vavylonis D, Pollard TD. 2007. Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy. Proc. Natl. Acad. Sci. USA 104:In press
    • (2007) Proc. Natl. Acad. Sci. USA , pp. 104
    • Fujiwara, I.1    Vavylonis, D.2    Pollard, T.D.3
  • 32
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homolog
    • Garner EC, Campbell CS, Mullins RD. 2004. Dynamic instability in a DNA-segregating prokaryotic actin homolog. Science 306:1021-25
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1    Campbell, C.S.2    Mullins, R.D.3
  • 35
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • Goley ED, Rodenbusch SE, Martin AC, Welch MD. 2004. Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor. Mol. Cell 16:269-79
    • (2004) Mol. Cell , vol.16 , pp. 269-279
    • Goley, E.D.1    Rodenbusch, S.E.2    Martin, A.C.3    Welch, M.D.4
  • 36
    • 34248154652 scopus 로고    scopus 로고
    • Goode BL, Eck MJ. 2007. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem, 76:In press
    • Goode BL, Eck MJ. 2007. Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem, 76:In press
  • 37
    • 0035972165 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the actin filament binding protein Abp1p
    • Goode BL, Rodal AA, Barnes G, Drubin DG. 2001. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J. Cell Biol. 153:627-34
    • (2001) J. Cell Biol , vol.153 , pp. 627-634
    • Goode, B.L.1    Rodal, A.A.2    Barnes, G.3    Drubin, D.G.4
  • 38
    • 0035930328 scopus 로고    scopus 로고
    • Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity
    • Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD. 2001. Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. Mol. Cell Biol. 8:1041-52
    • (2001) Mol. Cell Biol , vol.8 , pp. 1041-1052
    • Gournier, H.1    Goley, E.D.2    Niederstrasser, H.3    Trinh, T.4    Welch, M.D.5
  • 39
    • 2442473140 scopus 로고    scopus 로고
    • The mouse formin, FRLα, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
    • Harris ES, Li F, Higgs HN. 2004. The mouse formin, FRLα, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 279:20076-87
    • (2004) J. Biol. Chem , vol.279 , pp. 20076-20087
    • Harris, E.S.1    Li, F.2    Higgs, H.N.3
  • 40
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • Harris ES, Rouiller I, Hanein D, Higgs HN. 2006. Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 281:14383-92
    • (2006) J. Biol. Chem , vol.281 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 41
    • 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, et al. 2004. Actin polymerization-driven molecular movement of mDia1 in living cells. Science 303:2007-10
    • (2004) Science , vol.303 , pp. 2007-2010
    • Higashida, C.1    Miyoshi, T.2    Fujita, A.3    Oceguera-Yanez, F.4    Monypenny, J.5
  • 42
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: A domain-based approach
    • Higgs HN. 2005. Formin proteins: a domain-based approach. Trends Biochem. Sci. 30:342-53
    • (2005) Trends Biochem. Sci , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 43
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization
    • Higgs HN, Blanchoin L, Pollard TD. 1999. Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization. Biochemistry 38:15212-22
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 44
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho HY, Rohatgi R, Lebensohn AM, Le M, Li J, et al. 2004. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118:203-16
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Le, M.4    Li, J.5
  • 45
    • 0035949469 scopus 로고    scopus 로고
    • CR16 forms a complex with N-WASP in brain and is a novel member ofa conserved proline-rich actin-binding protein family
    • Ho HY, Rohatgi R, Ma L, Kirschner MW. 2001. CR16 forms a complex with N-WASP in brain and is a novel member ofa conserved proline-rich actin-binding protein family. Proc. Natl. Acad. Sci. USA 98:11306-11
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11306-11311
    • Ho, H.Y.1    Rohatgi, R.2    Ma, L.3    Kirschner, M.W.4
  • 47
    • 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, 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
  • 48
    • 27144493410 scopus 로고    scopus 로고
    • Abi1 regulates the activity of N-WASP and WAVE in distinct actin-based processes
    • Innocenti M, Gerboth S, Rottner K, Lai FP, Hertzog M, et al. 2005. Abi1 regulates the activity of N-WASP and WAVE in distinct actin-based processes. Nat. Cell Biol. 7:969-76
    • (2005) Nat. Cell Biol , vol.7 , pp. 969-976
    • Innocenti, M.1    Gerboth, S.2    Rottner, K.3    Lai, F.P.4    Hertzog, M.5
  • 49
    • 2342483041 scopus 로고    scopus 로고
    • Abi1 is essential for the formation and activation ofa WAVE2 signaling complex
    • Innocenti M, Zucconi A, Disanza A, Frittoli E, Areces LB, et al. 2004. Abi1 is essential for the formation and activation ofa WAVE2 signaling complex. Nat. Cell Biol. 6:319-27
    • (2004) Nat. Cell Biol , vol.6 , pp. 319-327
    • Innocenti, M.1    Zucconi, A.2    Disanza, A.3    Frittoli, E.4    Areces, L.B.5
  • 51
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen M, Sun Y, Drubin DG. 2003. A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115:475-87
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 52
  • 53
    • 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
    • Kelly AE, Kranitz H, Dotsch V, Mullins RD. 2006. 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. 281:10589-97
    • (2006) J. Biol. Chem , vol.281 , pp. 10589-10597
    • Kelly, A.E.1    Kranitz, H.2    Dotsch, V.3    Mullins, R.D.4
  • 54
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich Syndrome protein
    • Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK. 2000. Autoinhibition and activation mechanisms of the Wiskott-Aldrich Syndrome protein. Nature 404:151-58
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 55
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • Kovar DR. 2006. Molecular details of formin-mediated actin assembly. Curr. Opin. Cell Biol. 18:11-17
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 11-17
    • Kovar, DR.1
  • 56
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. 2006. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124:423-35
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 57
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • Kovar DR, Kuhn JR, Tichy AL, Pollard TD. 2003. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161:875-87
    • (2003) J. Cell Biol , vol.161 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 58
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar DR, Pollard TD. 2004. Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl. Acad. Sci. USA 101:14725-30
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 59
    • 18244377374 scopus 로고    scopus 로고
    • Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast
    • Kovar DR, Wu JQ, Pollard TD. 2005. Profilin-mediated competition between capping protein and formin Cdc12p during cytokinesis in fission yeast. Mol. Biol. Cell 16:2313-24
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2313-2324
    • Kovar, D.R.1    Wu, J.Q.2    Pollard, T.D.3
  • 60
    • 27944482589 scopus 로고    scopus 로고
    • NMR analyses of the activation of the Arp2/3 complex by neuronal Wiskott-Aldrich syndrome protein
    • Kreishman-Deitrick M, Goley ED, Burdine L, Denison C, Egile C, et al. 2005. NMR analyses of the activation of the Arp2/3 complex by neuronal Wiskott-Aldrich syndrome protein. Biochemistry 44:15247-56
    • (2005) Biochemistry , vol.44 , pp. 15247-15256
    • Kreishman-Deitrick, M.1    Goley, E.D.2    Burdine, L.3    Denison, C.4    Egile, C.5
  • 61
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn JR, Pollard TD. 2005. Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys. J. 88:1387-402
    • (2005) Biophys. J , vol.88 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 62
    • 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, 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. 13:1867-75
    • (2003) Curr. Biol , vol.13 , pp. 1867-1875
    • Kunda, P.1    Craig, G.2    Dominguez, V.3    Baum, B.4
  • 63
    • 0035861670 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex by Wiskott-Aldrich Syndrome protein is linked to enhanced binding of ATP to Arp2
    • Le Clainche C, Didry D, Carlier MF, Pantaloni C. 2001. Activation of Arp2/3 complex by Wiskott-Aldrich Syndrome protein is linked to enhanced binding of ATP to Arp2. J. Biol. Chem. 276:46689-92
    • (2001) J. Biol. Chem , vol.276 , pp. 46689-46692
    • Le Clainche, C.1    Didry, D.2    Carlier, M.F.3    Pantaloni, C.4
  • 64
    • 0038313144 scopus 로고    scopus 로고
    • ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays
    • Le Clainche C, Pantaloni C, Carlier MF. 2003. ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays. Proc. Natl. Acad. Sci. USA 100:6337-42
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6337-6342
    • Le Clainche, C.1    Pantaloni, C.2    Carlier, M.F.3
  • 65
    • 17644377914 scopus 로고    scopus 로고
    • The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein
    • Leung DW, Rosen MK. 2005. The nucleotide switch in Cdc42 modulates coupling between the GTPase-binding and allosteric equilibria of Wiskott-Aldrich syndrome protein. Proc. Natl. Acad. Sci. USA 102:5685-90
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5685-5690
    • Leung, D.W.1    Rosen, M.K.2
  • 66
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
    • Li F, Higgs HN. 2005. Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. J. Biol. Chem. 280:6986-92
    • (2005) J. Biol. Chem , vol.280 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 67
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel TP, Boujemaa R, Pantaloni D, Carlier MF. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401:613-16
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 69
    • 33751229634 scopus 로고    scopus 로고
    • Kinetics of the formation and dissociation of actin filament branches by Arp2/3 complex
    • Mahaffy RE, Pollard TD. 2006. Kinetics of the formation and dissociation of actin filament branches by Arp2/3 complex. Biophys. J. 91:3519-28
    • (2006) Biophys. J , vol.91 , pp. 3519-3528
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 70
    • 34347252820 scopus 로고    scopus 로고
    • Influence of phalloidin on the formation of actin filament branches bv Arp2/3 complex
    • In press
    • Mahaffy RE, Pollard TD. 2007. Influence of phalloidin on the formation of actin filament branches bv Arp2/3 complex. Biochemistry. In press
    • (2007) Biochemistry
    • Mahaffy, R.E.1    Pollard, T.D.2
  • 71
    • 0035146636 scopus 로고    scopus 로고
    • Interaction of WASp/Scar proteins with actin and vertebrate Arp2/3 complex
    • Marchand JB, Kaiser DA, Pollard TD, Higgs HN. 2001. Interaction of WASp/Scar proteins with actin and vertebrate Arp2/3 complex. Nat. Cell Biol. 3:76-82
    • (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
  • 72
    • 33746646463 scopus 로고    scopus 로고
    • Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation
    • Martin AC, Welch MD, Drubin DG. 2006. Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation. Nat. Cell Biol. 8:826-33
    • (2006) Nat. Cell Biol , vol.8 , pp. 826-833
    • Martin, A.C.1    Welch, M.D.2    Drubin, D.G.3
  • 73
    • 13844250532 scopus 로고    scopus 로고
    • Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function
    • Martin AC, Xu XP, Rouiller I, Kaksonen M, Sun Y, et al. 2005. Effects of Arp2 and Arp3 nucleotide-binding pocket mutations on Arp2/3 complex function. J. Cell Biol. 168:315-28
    • (2005) J. Cell Biol , vol.168 , pp. 315-328
    • Martin, A.C.1    Xu, X.P.2    Rouiller, I.3    Kaksonen, M.4    Sun, Y.5
  • 74
    • 0029661920 scopus 로고    scopus 로고
    • Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6mereapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay
    • Melki R, Fievez S, Carlier MF. 1996. Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6mereapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay. Biochemistry 35:12038-45
    • (1996) Biochemistry , vol.35 , pp. 12038-12045
    • Melki, R.1    Fievez, S.2    Carlier, M.F.3
  • 75
    • 27744591230 scopus 로고    scopus 로고
    • The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1
    • Michelot A, GuerinC, Fluang S, Ingouff M, Richard S, et al. 2005. The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1. Plant Cell 17:2296-313
    • (2005) Plant Cell , vol.17 , pp. 2296-2313
    • Michelot, A.1    Guerin, C.2    Fluang, S.3    Ingouff, M.4    Richard, S.5
  • 76
    • 33747830489 scopus 로고    scopus 로고
    • Quantitative modeling in cell biology: What is it good for?
    • Mogilner A, Wollman R, Marshall WF. 2006. Quantitative modeling in cell biology: What is it good for? Dev. Cell 11:279-87
    • (2006) Dev. Cell , vol.11 , pp. 279-287
    • Mogilner, A.1    Wollman, R.2    Marshall, W.F.3
  • 77
    • 0033780474 scopus 로고    scopus 로고
    • A complex of N-WASP and WIP integrates signaling cascades that lead to actin polymerization
    • Moreau V, Frischknecht F, Reckmann I, Vincentelli R, Rabut G, et al. 2000. A complex of N-WASP and WIP integrates signaling cascades that lead to actin polymerization. Nat. Cell Biol. 2:441-48
    • (2000) Nat. Cell Biol , vol.2 , pp. 441-448
    • Moreau, V.1    Frischknecht, F.2    Reckmann, I.3    Vincentelli, R.4    Rabut, G.5
  • 78
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • Moseley JB, Goode BL. 2005. Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J. Biol. Chem. 280:28023-33
    • (2005) J. Biol. Chem , vol.280 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 79
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • Moseley JB, Sagot I, Manning AL, Xu Y, Eck MJ, et al. 2004. A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15:896-907
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5
  • 81
    • 0033594548 scopus 로고    scopus 로고
    • Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts
    • Mullins RD, Pollard TD. 1999. Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Curr. Biol. 9:405-415
    • (1999) Curr. Biol , vol.9 , pp. 405-415
    • Mullins, R.D.1    Pollard, T.D.2
  • 82
    • 8144229871 scopus 로고    scopus 로고
    • Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
    • Nolen BJ, Littlefield RS, Pollard TD. 2004. Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proc. Natl. Acad. Sci. USA 101:15627-32
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15627-15632
    • Nolen, B.J.1    Littlefield, R.S.2    Pollard, T.D.3
  • 83
    • 34347246858 scopus 로고    scopus 로고
    • Insights into the influence of nucleotides on actin family proteins from seven new structures of Arp2/3 complex
    • In press
    • Nolen BJ, Pollard TD. 2007. Insights into the influence of nucleotides on actin family proteins from seven new structures of Arp2/3 complex. In press
    • (2007)
    • Nolen, B.J.1    Pollard, T.D.2
  • 84
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • Otomo T, Otomo C, Tomchick DR, Maehius M, Rosen MK. 2005. Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol. Cell 18:273-81
    • (2005) Mol. Cell , vol.18 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Maehius, M.4    Rosen, M.K.5
  • 85
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • Otomo T, Tomchick DR, Otomo C, Panchal SC, Maehius M, Rosen MK. 2005. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433:488-94
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Maehius, M.5    Rosen, M.K.6
  • 86
    • 0041989754 scopus 로고    scopus 로고
    • A conserved amphipathic helix in WASp/Scar proteins is essential for activation of Arp2/3 complex
    • Panchal SC, Kaiser DA, Torres E, Pollard TD, Rosen MK. 2003. A conserved amphipathic helix in WASp/Scar proteins is essential for activation of Arp2/3 complex. Nat. Struct. Biol. 10:591-98
    • (2003) Nat. Struct. Biol , vol.10 , pp. 591-598
    • Panchal, S.C.1    Kaiser, D.A.2    Torres, E.3    Pollard, T.D.4    Rosen, M.K.5
  • 87
    • 33744832052 scopus 로고    scopus 로고
    • Cortactin binding to F-actin revealed by electron microscopy and 3D reconstruction
    • Pant K, Chereau D, Hatch V, Dominguez R, Lehman W. 2006. Cortactin binding to F-actin revealed by electron microscopy and 3D reconstruction. J. Mol. Biol. 359:840-47
    • (2006) J. Mol. Biol , vol.359 , pp. 840-847
    • Pant, K.1    Chereau, D.2    Hatch, V.3    Dominguez, R.4    Lehman, W.5
  • 88
    • 34347215640 scopus 로고    scopus 로고
    • How profilin and FH1 domains regulate processive actin filament elongation by formin FH2 domains
    • In press
    • Paul A, Pollard TD. 2007. How profilin and FH1 domains regulate processive actin filament elongation by formin FH2 domains. In press
    • (2007)
    • Paul, A.1    Pollard, T.D.2
  • 89
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation
    • Petersen J, Nielsen O, Egel R, Hagan IM. 1998. FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J. Cell Biol. 141:1217-28
    • (1998) J. Cell Biol , vol.141 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 90
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD. 1986. Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J. Cell Biol. 103:2747-54
    • (1986) J. Cell Biol , vol.103 , pp. 2747-2754
    • Pollard, T.D.1
  • 92
    • 34347256276 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 93
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-65
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 94
    • 34347226086 scopus 로고    scopus 로고
    • New York: Saunders/Elsevier, pp, 2nd ed
    • Pollard TD, Earnshaw WC. 2007. Cell Biology. New York: Saunders/Elsevier, pp. 902. 2nd ed.
    • (2007) Cell Biology , pp. 902
    • Pollard, T.D.1    Earnshaw, W.C.2
  • 96
    • 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, et al. 2002. Role of formins in actin assembly: nucleation and barbed end association. Science 297:612-15
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1    Evangelista, M.2    Yang, C.3    Bi, E.4    Zigmond, S.5
  • 98
    • 33344457987 scopus 로고    scopus 로고
    • WASP suppresses the growth defect of Saccharomyces cerevisiae las 17 Delta strain in the presence of WIP
    • Rajmohan R, Meng L, Yu S, Thanabalu T. 2006. WASP suppresses the growth defect of Saccharomyces cerevisiae las 17 Delta strain in the presence of WIP. Biochem. Biophys. Res. Commun. 342:529-36
    • (2006) Biochem. Biophys. Res. Commun , vol.342 , pp. 529-536
    • Rajmohan, R.1    Meng, L.2    Yu, S.3    Thanabalu, T.4
  • 100
    • 0037599264 scopus 로고    scopus 로고
    • Negative regulation of yeast WASp by two SH3 domain-containing proteins
    • Rodal AA, Manning AL, Goode BL, Drubin DG. 2003. Negative regulation of yeast WASp by two SH3 domain-containing proteins. Curr. Biol. 13:1000-8
    • (2003) Curr. Biol , vol.13 , pp. 1000-1008
    • Rodal, A.A.1    Manning, A.L.2    Goode, B.L.3    Drubin, D.G.4
  • 102
    • 0035854732 scopus 로고    scopus 로고
    • Nek and phosphatidylinositol 4,5-bisphosphate synergistieally activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ. 2001. Nek and phosphatidylinositol 4,5-bisphosphate synergistieally activate actin polymerization through the N-WASP-Arp2/3 pathway. J. Biol. Chem. 276:26448-52
    • (2001) J. Biol. Chem , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 103
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero S, Le Clainche C, Didry D, Egile C, Pantaloni D, Carlier MF. 2004. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119:419-29
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 104
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R, Weyand M, Lammers M, Ishizaki T, Ahmadian MR, Wittinghofer A. 2005. Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435:513-18
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 105
    • 34347255894 scopus 로고    scopus 로고
    • Structural basis for the formation of actin branch junctions by Arp2/3 complex
    • In press
    • Rouiller I, Xu XP, Amann KJ, Egile C, Nicastro D, et al. 2007. Structural basis for the formation of actin branch junctions by Arp2/3 complex. In press
    • (2007)
    • Rouiller, I.1    Xu, X.P.2    Amann, K.J.3    Egile, C.4    Nicastro, D.5
  • 106
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I, Klee SK, Pellman D. 2002. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4:42-50
    • (2002) Nat. Cell Biol , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 108
    • 0034896467 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of actin filament nucleation
    • Sept D, McCammon JA. 2001. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81:667-74
    • (2001) Biophys. J , vol.81 , pp. 667-674
    • Sept, D.1    McCammon, J.A.2
  • 109
    • 33748123994 scopus 로고    scopus 로고
    • Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLα and mDia1
    • Seth A, Otomo C, Rosen MK. 2006. Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLα and mDia1. J Cell Biol. 174:701-13
    • (2006) J Cell Biol , vol.174 , pp. 701-713
    • Seth, A.1    Otomo, C.2    Rosen, M.K.3
  • 110
    • 24944560068 scopus 로고    scopus 로고
    • A novel mechanism of actin filament processive capping by formin: Solution of the rotation paradox
    • Shemesh T, Otomo T, Rosen MK, Bershadsky AD, Kozlov MM. 2005. A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox. J. Cell Biol. 170:889-93
    • (2005) J. Cell Biol , vol.170 , pp. 889-893
    • Shemesh, T.1    Otomo, T.2    Rosen, M.K.3    Bershadsky, A.D.4    Kozlov, M.M.5
  • 111
    • 23944492960 scopus 로고    scopus 로고
    • Interactions of WASp, myosinI, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast
    • Sirotkin V, Beltzner C, Marchand JB, Pollard TD. 2005. Interactions of WASp, myosinI, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast. J. Cell Biol. 170:637-48
    • (2005) J. Cell Biol , vol.170 , pp. 637-648
    • Sirotkin, V.1    Beltzner, C.2    Marchand, J.B.3    Pollard, T.D.4
  • 112
    • 0036840975 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro
    • Soulard A, Lechler T, Spiridonov V, Shevchenko A, Li R, Winsor B. 2002. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol. Cell Biol. 22:7889-906
    • (2002) Mol. Cell Biol , vol.22 , pp. 7889-7906
    • Soulard, A.1    Lechler, T.2    Spiridonov, V.3    Shevchenko, A.4    Li, R.5    Winsor, B.6
  • 113
    • 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, et al. 2004. Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia formation. EMBO J. 23:749-59
    • (2004) EMBO J , vol.23 , pp. 749-759
    • Steffen, A.1    Rottner, K.2    Ehinger, J.3    Innocenti, M.4    Scita, G.5
  • 114
    • 22144490590 scopus 로고    scopus 로고
    • Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2
    • Stovold CF, Millard TH, Machesky LM. 2005. Inclusion of Scar/WAVE3 in a similar complex to Scar/WAVE1 and 2. BMC Cell Biol. 6:11
    • (2005) BMC Cell Biol , vol.6 , pp. 11
    • Stovold, C.F.1    Millard, T.H.2    Machesky, L.M.3
  • 115
    • 30844466190 scopus 로고    scopus 로고
    • Protein complexes regulating Arp2/3-mediated actin assembly
    • Stradal TE, Scita G. 2006. Protein complexes regulating Arp2/3-mediated actin assembly. Curr. Opin. Cell Biol. 18:4-10
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 4-10
    • Stradal, T.E.1    Scita, G.2
  • 116
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac
    • Suetsugu S, Kurisu S, Oikawa T, Yamazaki D, Oda A, Takenawa T. 2006. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. J. Cell Biol. 173:571-85
    • (2006) J. Cell Biol , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 117
    • 33745535568 scopus 로고    scopus 로고
    • Endocytic internalization in buddingyeast requires coordinated actin nucleation and myosin motor activity
    • Sun Y, Martin AC, Drubin DG. 2006. Endocytic internalization in buddingyeast requires coordinated actin nucleation and myosin motor activity. Dev. Cell 11:33-46
    • (2006) Dev. Cell , vol.11 , pp. 33-46
    • Sun, Y.1    Martin, A.C.2    Drubin, D.G.3
  • 121
  • 123
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar BJ, Alberts AS. 2003. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13:435-46
    • (2003) Trends Cell Biol , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 125
    • 0035814938 scopus 로고    scopus 로고
    • Cortaetin promotes and stabilizes Arp2/3-induced actin filament network formation
    • Weaver AM, Karginov AV, Kinley AW, Weed SA, Li Y, et al. 2001. Cortaetin promotes and stabilizes Arp2/3-induced actin filament network formation. Curr. Biol. 11:370-74
    • (2001) Curr. Biol , vol.11 , pp. 370-374
    • Weaver, A.M.1    Karginov, A.V.2    Kinley, A.W.3    Weed, S.A.4    Li, Y.5
  • 126
    • 0017176529 scopus 로고
    • Head to tail polymerization of actin
    • Wegner A. 1976. Head to tail polymerization of actin. J. Mol. Biol. 108:139-50
    • (1976) J. Mol. Biol , vol.108 , pp. 139-150
    • Wegner, A.1
  • 128
    • 21244446303 scopus 로고    scopus 로고
    • Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require an Arp2/3-activating protein
    • Wen KK, Rubenstein PA. 2005. Acceleration of yeast actin polymerization by yeast Arp2/3 complex does not require an Arp2/3-activating protein. J. Biol. Chem. 280:24168-74
    • (2005) J. Biol. Chem , vol.280 , pp. 24168-24174
    • Wen, K.K.1    Rubenstein, P.A.2
  • 129
    • 34347245417 scopus 로고    scopus 로고
    • Three-dimensional structure of Arp2/3 complex with bound nucleation promoting factors
    • In press
    • Xu SP, Rouiller I, Egile C, Kim E, Pollard TD, et al. 2007. Three-dimensional structure of Arp2/3 complex with bound nucleation promoting factors. In press
    • (2007)
    • Xu, S.P.1    Rouiller, I.2    Egile, C.3    Kim, E.4    Pollard, T.D.5
  • 130
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu Y, Moseley JB, Sagot I, Poy F, Pellman D, et al. 2004. Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116:711-23
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5
  • 132
    • 33646013893 scopus 로고    scopus 로고
    • Profilin: Emerging concepts and lingering misconceptions
    • Yarmola EG, Bubb MR. 2006. Profilin: emerging concepts and lingering misconceptions. Trends Biochem. Sci. 31:197-205
    • (2006) Trends Biochem. Sci , vol.31 , pp. 197-205
    • Yarmola, E.G.1    Bubb, M.R.2
  • 133
    • 0035793587 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the Listeria ActA protein: ActA binds two actin monomers and three subunits of the Arp2/3 complex
    • Zalevsky J, Grigorova I, Mullins RD. 2001. Activation of the Arp2/3 complex by the Listeria ActA protein: ActA binds two actin monomers and three subunits of the Arp2/3 complex. J. Biol. Chem. 276:3468-75
    • (2001) J. Biol. Chem , vol.276 , pp. 3468-3475
    • Zalevsky, J.1    Grigorova, I.2    Mullins, R.D.3
  • 134
    • 0142136092 scopus 로고    scopus 로고
    • Formin leaky cap allows elongation in the presence of tight capping proteins
    • Zigmond SH, Evangelista M, Boone C, Yang C, Dar AC, et al. 2003. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr. Biol. 13:1820-23
    • (2003) Curr. Biol , vol.13 , pp. 1820-1823
    • Zigmond, S.H.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Dar, A.C.5
  • 135
    • 0032563603 scopus 로고    scopus 로고
    • Mechanism of Cdc42-induced actin polymerization in neutrophil extracts
    • Zigmond SH, Joyce M, Yang C, Brown K, Huang M, Pring M. 1998. Mechanism of Cdc42-induced actin polymerization in neutrophil extracts. J. Cell Biol. 142:1001-12
    • (1998) J. Cell Biol , vol.142 , pp. 1001-1012
    • Zigmond, S.H.1    Joyce, M.2    Yang, C.3    Brown, K.4    Huang, M.5    Pring, M.6


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