메뉴 건너뛰기




Volumn 23, Issue 20, 2013, Pages 1990-1998

Dip1 defines a class of Arp2/3 complex activators that function without preformed actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; DIP1 PROTEIN, S POMBE; SCHIZOSACCHAROMYCES POMBE PROTEIN;

EID: 84886287854     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2013.08.029     Document Type: Article
Times cited : (62)

References (47)
  • 2
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: Mechanisms and interplay
    • M.A. Chesarone, and B.L. Goode Actin nucleation and elongation factors: mechanisms and interplay Curr. Opin. Cell Biol. 21 2009 28 37
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 3
    • 33749037156 scopus 로고    scopus 로고
    • The ARP2/3 complex: An actin nucleator comes of age
    • E.D. Goley, and 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
  • 4
    • 84871519238 scopus 로고    scopus 로고
    • New insights into the regulation and cellular functions of the ARP2/3 complex
    • J.D. Rotty, C. Wu, and J.E. Bear New insights into the regulation and cellular functions of the ARP2/3 complex Nat. Rev. Mol. Cell Biol. 14 2013 7 12
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 7-12
    • Rotty, J.D.1    Wu, C.2    Bear, J.E.3
  • 5
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • D. Chereau, F. Kerff, P. Graceffa, Z. Grabarek, K. Langsetmo, and R. Dominguez Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly Proc. Natl. Acad. Sci. USA 102 2005 16644 16649
    • (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
  • 6
    • 84878261069 scopus 로고    scopus 로고
    • Small molecules CK-666 and CK-869 inhibit actin-related protein 2/3 complex by blocking an activating conformational change
    • B. Hetrick, M.S. Han, L.A. Helgeson, and B.J. Nolen Small molecules CK-666 and CK-869 inhibit actin-related protein 2/3 complex by blocking an activating conformational change Chem. Biol. 20 2013 701 712
    • (2013) Chem. Biol. , vol.20 , pp. 701-712
    • Hetrick, B.1    Han, M.S.2    Helgeson, L.A.3    Nolen, B.J.4
  • 8
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • J.H. Iwasa, and 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
  • 9
    • 79960666093 scopus 로고    scopus 로고
    • Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast
    • C.T. Skau, D.S. Courson, A.J. Bestul, J.D. Winkelman, R.S. Rock, V. Sirotkin, and D.R. Kovar Actin filament bundling by fimbrin is important for endocytosis, cytokinesis, and polarization in fission yeast J. Biol. Chem. 286 2011 26964 26977
    • (2011) J. Biol. Chem. , vol.286 , pp. 26964-26977
    • Skau, C.T.1    Courson, D.S.2    Bestul, A.J.3    Winkelman, J.D.4    Rock, R.S.5    Sirotkin, V.6    Kovar, D.R.7
  • 10
    • 79955785854 scopus 로고    scopus 로고
    • Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin
    • S.L. Liu, K.M. Needham, J.R. May, and B.J. Nolen Mechanism of a concentration-dependent switch between activation and inhibition of Arp2/3 complex by coronin J. Biol. Chem. 286 2011 17039 17046
    • (2011) J. Biol. Chem. , vol.286 , pp. 17039-17046
    • Liu, S.L.1    Needham, K.M.2    May, J.R.3    Nolen, B.J.4
  • 11
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • L. Blanchoin, T.D. Pollard, and S.E. Hitchcock-DeGregori Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin Curr. Biol. 11 2001 1300 1304
    • (2001) Curr. Biol. , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-Degregori, S.E.3
  • 13
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42
    • M. Fukuoka, S. Suetsugu, H. Miki, K. Fukami, T. Endo, and T. Takenawa A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, induces Arp2/3 complex activation independent of Cdc42 J. Cell Biol. 152 2001 471 482
    • (2001) J. Cell Biol. , vol.152 , pp. 471-482
    • Fukuoka, M.1    Suetsugu, S.2    Miki, H.3    Fukami, K.4    Endo, T.5    Takenawa, T.6
  • 14
    • 79958056950 scopus 로고    scopus 로고
    • Characterization of dip1p reveals a switch in Arp2/3-dependent actin assembly for fission yeast endocytosis
    • R. Basu, and F. Chang Characterization of dip1p reveals a switch in Arp2/3-dependent actin assembly for fission yeast endocytosis Curr. Biol. 21 2011 905 916
    • (2011) Curr. Biol. , vol.21 , pp. 905-916
    • Basu, R.1    Chang, F.2
  • 15
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • M. Kaksonen, C.P. Toret, and D.G. Drubin Harnessing actin dynamics for clathrin-mediated endocytosis Nat. Rev. Mol. Cell Biol. 7 2006 404 414
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 16
    • 77955647583 scopus 로고    scopus 로고
    • Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast
    • V. Sirotkin, J. Berro, K. Macmillan, L. Zhao, and T.D. Pollard Quantitative analysis of the mechanism of endocytic actin patch assembly and disassembly in fission yeast Mol. Biol. Cell 21 2010 2894 2904
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2894-2904
    • Sirotkin, V.1    Berro, J.2    Macmillan, K.3    Zhao, L.4    Pollard, T.D.5
  • 17
    • 23944492960 scopus 로고    scopus 로고
    • Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast
    • V. Sirotkin, C.C. Beltzner, J.B. Marchand, and T.D. Pollard Interactions of WASp, myosin-I, and verprolin with Arp2/3 complex during actin patch assembly in fission yeast J. Cell Biol. 170 2005 637 648
    • (2005) J. Cell Biol. , vol.170 , pp. 637-648
    • Sirotkin, V.1    Beltzner, C.C.2    Marchand, J.B.3    Pollard, T.D.4
  • 18
    • 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, and 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
  • 20
    • 84884676960 scopus 로고    scopus 로고
    • Mechanism of synergistic activation of Arp2/3 complex by cortactin and N-WASP
    • L.A. Helgeson, and B.J. Nolen Mechanism of synergistic activation of Arp2/3 complex by cortactin and N-WASP Elife 2 2013 e00884
    • (2013) Elife , vol.2 , pp. 00884
    • Helgeson, L.A.1    Nolen, B.J.2
  • 21
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • S.C. Mockrin, and E.D. Korn Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate Biochemistry 19 1980 5359 5362
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 22
    • 0019973904 scopus 로고
    • Mechanism of action of Acanthamoeba profilin: Demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2
    • P.C. Tseng, and T.D. Pollard Mechanism of action of Acanthamoeba profilin: demonstration of actin species specificity and regulation by micromolar concentrations of MgCl2 J. Cell Biol. 94 1982 213 218
    • (1982) J. Cell Biol. , vol.94 , pp. 213-218
    • Tseng, P.C.1    Pollard, T.D.2
  • 24
    • 0037599264 scopus 로고    scopus 로고
    • Negative regulation of yeast WASp by two SH3 domain-containing proteins
    • A.A. Rodal, A.L. Manning, B.L. Goode, and D.G. Drubin Negative regulation of yeast WASp by two SH3 domain-containing proteins Curr. Biol. 13 2003 1000 1008
    • (2003) Curr. Biol. , vol.13 , pp. 1000-1008
    • Rodal, A.A.1    Manning, A.L.2    Goode, B.L.3    Drubin, D.G.4
  • 25
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • J. Zalevsky, L. Lempert, H. Kranitz, and R.D. Mullins Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities Curr. Biol. 11 2001 1903 1913
    • (2001) Curr. Biol. , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 26
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • L. Blanchoin, K.J. Amann, H.N. Higgs, J.B. Marchand, D.A. Kaiser, and T.D. Pollard Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins Nature 404 2000 1007 1011
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 27
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • S.C. Ti, C.T. Jurgenson, B.J. Nolen, and T.D. Pollard Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex Proc. Natl. Acad. Sci. USA 108 2011 E463 E471
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108
    • Ti, S.C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 28
    • 46149096223 scopus 로고    scopus 로고
    • WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport
    • K.G. Campellone, N.J. Webb, E.A. Znameroski, and M.D. Welch WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport Cell 134 2008 148 161
    • (2008) Cell , vol.134 , pp. 148-161
    • Campellone, K.G.1    Webb, N.J.2    Znameroski, E.A.3    Welch, M.D.4
  • 29
    • 34247584045 scopus 로고    scopus 로고
    • F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation
    • D.J. Kim, S.H. Kim, S.M. Kim, J.I. Bae, J. Ahnn, and W.K. Song F-actin binding region of SPIN90 C-terminus is essential for actin polymerization and lamellipodia formation Cell Commun. Adhes. 14 2007 33 43
    • (2007) Cell Commun. Adhes. , vol.14 , pp. 33-43
    • Kim, D.J.1    Kim, S.H.2    Kim, S.M.3    Bae, J.I.4    Ahnn, J.5    Song, W.K.6
  • 30
    • 33745003433 scopus 로고    scopus 로고
    • Dynamics of the formin for3p in actin cable assembly
    • S.G. Martin, and F. Chang Dynamics of the formin for3p in actin cable assembly Curr. Biol. 16 2006 1161 1170
    • (2006) Curr. Biol. , vol.16 , pp. 1161-1170
    • Martin, S.G.1    Chang, F.2
  • 31
    • 0035090345 scopus 로고    scopus 로고
    • Role of actin polymerization and actin cables in actin-patch movement in Schizosaccharomyces pombe
    • R.J. Pelham Jr., and F. Chang Role of actin polymerization and actin cables in actin-patch movement in Schizosaccharomyces pombe Nat. Cell Biol. 3 2001 235 244
    • (2001) Nat. Cell Biol. , vol.3 , pp. 235-244
    • Pelham, Jr.R.J.1    Chang, F.2
  • 32
    • 34249751177 scopus 로고    scopus 로고
    • Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe
    • K. Skoumpla, A.T. Coulton, W. Lehman, M.A. Geeves, and D.P. Mulvihill Acetylation regulates tropomyosin function in the fission yeast Schizosaccharomyces pombe J. Cell Sci. 120 2007 1635 1645
    • (2007) J. Cell Sci. , vol.120 , pp. 1635-1645
    • Skoumpla, K.1    Coulton, A.T.2    Lehman, W.3    Geeves, M.A.4    Mulvihill, D.P.5
  • 33
    • 77957850795 scopus 로고    scopus 로고
    • Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast
    • C.T. Skau, and D.R. Kovar Fimbrin and tropomyosin competition regulates endocytosis and cytokinesis kinetics in fission yeast Curr. Biol. 20 2010 1415 1422
    • (2010) Curr. Biol. , vol.20 , pp. 1415-1422
    • Skau, C.T.1    Kovar, D.R.2
  • 34
    • 0031685559 scopus 로고    scopus 로고
    • Subcellular localization and possible function of actin, tropomyosin and actin-related protein 3 (Arp3) in the fission yeast Schizosaccharomyces pombe
    • R. Arai, K. Nakano, and I. Mabuchi Subcellular localization and possible function of actin, tropomyosin and actin-related protein 3 (Arp3) in the fission yeast Schizosaccharomyces pombe Eur. J. Cell Biol. 76 1998 288 295
    • (1998) Eur. J. Cell Biol. , vol.76 , pp. 288-295
    • Arai, R.1    Nakano, K.2    Mabuchi, I.3
  • 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, and 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
  • 38
    • 4444254413 scopus 로고    scopus 로고
    • Yeast actin patches are networks of branched actin filaments
    • M.E. Young, J.A. Cooper, and P.C. Bridgman Yeast actin patches are networks of branched actin filaments J. Cell Biol. 166 2004 629 635
    • (2004) J. Cell Biol. , vol.166 , pp. 629-635
    • Young, M.E.1    Cooper, J.A.2    Bridgman, P.C.3
  • 39
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • B.L. Goode, and M.J. Eck Mechanism and function of formins in the control of actin assembly Annu. Rev. Biochem. 76 2007 593 627
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 40
    • 84873411382 scopus 로고    scopus 로고
    • A novel actin-binding motif in Las17/WASP nucleates actin filaments independently of Arp2/3
    • A.N. Urbanek, A.P. Smith, E.G. Allwood, W.I. Booth, and K.R. Ayscough A novel actin-binding motif in Las17/WASP nucleates actin filaments independently of Arp2/3 Curr. Biol. 23 2013 196 203
    • (2013) Curr. Biol. , vol.23 , pp. 196-203
    • Urbanek, A.N.1    Smith, A.P.2    Allwood, E.G.3    Booth, W.I.4    Ayscough, K.R.5
  • 41
    • 84879965317 scopus 로고    scopus 로고
    • Actin filament severing by cofilin dismantles actin patches and produces mother filaments for new patches
    • Q. Chen, and T.D. Pollard Actin filament severing by cofilin dismantles actin patches and produces mother filaments for new patches Curr. Biol. 23 2013 1154 1162
    • (2013) Curr. Biol. , vol.23 , pp. 1154-1162
    • Chen, Q.1    Pollard, T.D.2
  • 42
    • 79952104296 scopus 로고    scopus 로고
    • Three's company: The fission yeast actin cytoskeleton
    • D.R. Kovar, V. Sirotkin, and M. Lord Three's company: the fission yeast actin cytoskeleton Trends Cell Biol. 21 2011 177 187
    • (2011) Trends Cell Biol. , vol.21 , pp. 177-187
    • Kovar, D.R.1    Sirotkin, V.2    Lord, M.3
  • 44
    • 38949214078 scopus 로고    scopus 로고
    • Distinct roles for Arp2/3 regulators in actin assembly and endocytosis
    • B.J. Galletta, D.Y. Chuang, and J.A. Cooper Distinct roles for Arp2/3 regulators in actin assembly and endocytosis PLoS Biol. 6 2008 e1
    • (2008) PLoS Biol. , vol.6 , pp. 1
    • Galletta, B.J.1    Chuang, D.Y.2    Cooper, J.A.3
  • 45
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • S. MacLean-Fletcher, and T.D. Pollard Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association Biochem. Biophys. Res. Commun. 96 1980 18 27
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 18-27
    • Maclean-Fletcher, S.1    Pollard, T.D.2
  • 46
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • T.D. Pollard Polymerization of ADP-actin J. Cell Biol. 99 1984 769 777
    • (1984) J. Cell Biol. , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 47
    • 84872053443 scopus 로고    scopus 로고
    • Insertions within the actin core of actin-related protein 3 (Arp3) modulate branching nucleation by Arp2/3 complex
    • S.L. Liu, J.R. May, L.A. Helgeson, and B.J. Nolen Insertions within the actin core of actin-related protein 3 (Arp3) modulate branching nucleation by Arp2/3 complex J. Biol. Chem. 288 2013 487 497
    • (2013) J. Biol. Chem. , vol.288 , pp. 487-497
    • Liu, S.L.1    May, J.R.2    Helgeson, L.A.3    Nolen, B.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.