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Volumn 23, Issue 12, 2013, Pages 1037-1045

GMF severs actin-Arp2/3 complex branch junctions by a cofilin-like mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; COFILIN 1; GLIA MATURATION FACTOR; GLIA MATURATION FACTOR GAMMA; GMF1 PROTEIN, S POMBE; NERVE GROWTH FACTOR; SACCHAROMYCES CEREVISIAE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN;

EID: 84879309319     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2013.04.058     Document Type: Article
Times cited : (60)

References (49)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • M.D. Welch, J. Rosenblatt, J. Skoble, D.A. Portnoy, and T.J. Mitchison Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation Science 281 1998 105 108
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 4
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • L.M. Machesky, and R.H. Insall Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex Curr. Biol. 8 1998 1347 1356
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 6
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • S.L. Rogers, U. Wiedemann, N. Stuurman, and R.D. Vale Molecular requirements for actin-based lamella formation in Drosophila S2 cells J. Cell Biol. 162 2003 1079 1088
    • (2003) J. Cell Biol. , vol.162 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 8
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • P. Lappalainen, and D.G. Drubin Cofilin promotes rapid actin filament turnover in vivo Nature 388 1997 78 82
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 11
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • A. McGough, B. Pope, W. Chiu, and A. Weeds Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function J. Cell Biol. 138 1997 771 781
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 12
    • 0034687235 scopus 로고    scopus 로고
    • Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • L. Blanchoin, T.D. Pollard, and R.D. Mullins Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks Curr. Biol. 10 2000 1273 1282
    • (2000) Curr. Biol. , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 16
    • 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
  • 17
    • 64049091643 scopus 로고    scopus 로고
    • Cofilin dissociates Arp2/3 complex and branches from actin filaments
    • C. Chan, C.C. Beltzner, and T.D. Pollard Cofilin dissociates Arp2/3 complex and branches from actin filaments Curr. Biol. 19 2009 537 545
    • (2009) Curr. Biol. , vol.19 , pp. 537-545
    • Chan, C.1    Beltzner, C.C.2    Pollard, T.D.3
  • 18
    • 80052990415 scopus 로고    scopus 로고
    • Actin-depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics
    • M. Poukkula, E. Kremneva, M. Serlachius, and P. Lappalainen Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics Cytoskeleton (Hoboken) 68 2011 471 490
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 471-490
    • Poukkula, M.1    Kremneva, E.2    Serlachius, M.3    Lappalainen, P.4
  • 20
    • 33747390456 scopus 로고    scopus 로고
    • Glia maturation factor-gamma is preferentially expressed in microvascular endothelial and inflammatory cells and modulates actin cytoskeleton reorganization
    • K. Ikeda, R.K. Kundu, S. Ikeda, M. Kobara, H. Matsubara, and T. Quertermous Glia maturation factor-gamma is preferentially expressed in microvascular endothelial and inflammatory cells and modulates actin cytoskeleton reorganization Circ. Res. 99 2006 424 433
    • (2006) Circ. Res. , vol.99 , pp. 424-433
    • Ikeda, K.1    Kundu, R.K.2    Ikeda, S.3    Kobara, M.4    Matsubara, H.5    Quertermous, T.6
  • 21
    • 77953582940 scopus 로고    scopus 로고
    • GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton
    • K. Nakano, H. Kuwayama, M. Kawasaki, O. Numata, and M. Takaine GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton Cytoskeleton (Hoboken) 67 2010 373 382
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 373-382
    • Nakano, K.1    Kuwayama, H.2    Kawasaki, M.3    Numata, O.4    Takaine, M.5
  • 23
    • 0030880186 scopus 로고    scopus 로고
    • Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis
    • P. Lappalainen, E.V. Fedorov, A.A. Fedorov, S.C. Almo, and D.G. Drubin Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis EMBO J. 16 1997 5520 5530
    • (1997) EMBO J. , vol.16 , pp. 5520-5530
    • Lappalainen, P.1    Fedorov, E.V.2    Fedorov, A.A.3    Almo, S.C.4    Drubin, D.G.5
  • 25
    • 0035951069 scopus 로고    scopus 로고
    • Identification of yeast cofilin residues specific for actin monomer and PIP2 binding
    • P.J. Ojala, V. Paavilainen, and P. Lappalainen Identification of yeast cofilin residues specific for actin monomer and PIP2 binding Biochemistry 40 2001 15562 15569
    • (2001) Biochemistry , vol.40 , pp. 15562-15569
    • Ojala, P.J.1    Paavilainen, V.2    Lappalainen, P.3
  • 27
    • 47549090623 scopus 로고    scopus 로고
    • Structure of the actin-depolymerizing factor homology domain in complex with actin
    • V.O. Paavilainen, E. Oksanen, A. Goldman, and P. Lappalainen Structure of the actin-depolymerizing factor homology domain in complex with actin J. Cell Biol. 182 2008 51 59
    • (2008) J. Cell Biol. , vol.182 , pp. 51-59
    • Paavilainen, V.O.1    Oksanen, E.2    Goldman, A.3    Lappalainen, P.4
  • 31
    • 77953002874 scopus 로고    scopus 로고
    • Diffusion of the reaction boundary of rapidly interacting macromolecules in sedimentation velocity
    • P. Schuck Diffusion of the reaction boundary of rapidly interacting macromolecules in sedimentation velocity Biophys. J. 98 2010 2741 2751
    • (2010) Biophys. J. , vol.98 , pp. 2741-2751
    • Schuck, P.1
  • 32
    • 11144226715 scopus 로고    scopus 로고
    • ARPC1/Arc40 mediates the interaction of the actin-related protein 2 and 3 complex with Wiskott-Aldrich syndrome protein family activators
    • F. Pan, C. Egile, T. Lipkin, and R. Li ARPC1/Arc40 mediates the interaction of the actin-related protein 2 and 3 complex with Wiskott-Aldrich syndrome protein family activators J. Biol. Chem. 279 2004 54629 54636
    • (2004) J. Biol. Chem. , vol.279 , pp. 54629-54636
    • Pan, F.1    Egile, C.2    Lipkin, T.3    Li, R.4
  • 35
    • 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
  • 36
    • 80053311771 scopus 로고    scopus 로고
    • The interaction of cofilin with the actin filament
    • D.Y. Wong, and D. Sept The interaction of cofilin with the actin filament J. Mol. Biol. 413 2011 97 105
    • (2011) J. Mol. Biol. , vol.413 , pp. 97-105
    • Wong, D.Y.1    Sept, D.2
  • 37
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • E. Andrianantoandro, and T.D. Pollard Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin Mol. Cell 24 2006 13 23
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 38
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • L. Blanchoin, and T.D. Pollard Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin J. Biol. Chem. 273 1998 25106 25111
    • (1998) J. Biol. Chem. , vol.273 , pp. 25106-25111
    • Blanchoin, L.1    Pollard, T.D.2
  • 39
  • 40
    • 8144229871 scopus 로고    scopus 로고
    • Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
    • B.J. Nolen, R.S. Littlefield, and T.D. Pollard Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP Proc. Natl. Acad. Sci. USA 101 2004 15627 15632
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15627-15632
    • Nolen, B.J.1    Littlefield, R.S.2    Pollard, T.D.3
  • 43
    • 65549103882 scopus 로고    scopus 로고
    • Coronin switches roles in actin disassembly depending on the nucleotide state of actin
    • M. Gandhi, V. Achard, L. Blanchoin, and B.L. Goode Coronin switches roles in actin disassembly depending on the nucleotide state of actin Mol. Cell 34 2009 364 374
    • (2009) Mol. Cell , vol.34 , pp. 364-374
    • Gandhi, M.1    Achard, V.2    Blanchoin, L.3    Goode, B.L.4
  • 45
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 47
    • 0025181840 scopus 로고
    • Zero-length crosslinking procedure with the use of active esters
    • Z. Grabarek, and J. Gergely Zero-length crosslinking procedure with the use of active esters Anal. Biochem. 185 1990 131 135
    • (1990) Anal. Biochem. , vol.185 , pp. 131-135
    • Grabarek, Z.1    Gergely, J.2
  • 48
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: A comparison of the in vivo and structural roles of individual subunits
    • D.C. Winter, E.Y. Choe, and R. Li Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits Proc. Natl. Acad. Sci. USA 96 1999 7288 7293
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7288-7293
    • Winter, D.C.1    Choe, E.Y.2    Li, R.3
  • 49
    • 47749139334 scopus 로고    scopus 로고
    • Functional surfaces on the p35/ARPC2 subunit of Arp2/3 complex required for cell growth, actin nucleation, and endocytosis
    • K.M. Daugherty, and B.L. Goode Functional surfaces on the p35/ARPC2 subunit of Arp2/3 complex required for cell growth, actin nucleation, and endocytosis J. Biol. Chem. 283 2008 16950 16959
    • (2008) J. Biol. Chem. , vol.283 , pp. 16950-16959
    • Daugherty, K.M.1    Goode, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.