메뉴 건너뛰기




Volumn 26, Issue 3, 2007, Pages 449-457

Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex

Author keywords

CELLBIO

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 2-3 COMPLEX; ACTIN RELATED PROTEIN 3; ADENINE NUCLEOTIDE DERIVATIVE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CATION; GLUTARALDEHYDE; NUCLEOTIDE DERIVATIVE;

EID: 34247619703     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.04.017     Document Type: Article
Times cited : (64)

References (39)
  • 1
    • 0033524402 scopus 로고    scopus 로고
    • A change in actin conformation associated with filament instability after Pi release
    • Belmont L.D., Orlova A., Drubin D.G., and Egelman E.H. A change in actin conformation associated with filament instability after Pi release. Proc. Natl. Acad. Sci. USA 96 (1999) 29-34
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 29-34
    • Belmont, L.D.1    Orlova, A.2    Drubin, D.G.3    Egelman, E.H.4
  • 2
    • 0742289599 scopus 로고    scopus 로고
    • Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species
    • Beltzner C.C., and Pollard T.D. Identification of functionally important residues of Arp2/3 complex by analysis of homology models from diverse species. J. Mol. Biol. 336 (2004) 551-565
    • (2004) J. Mol. Biol. , vol.336 , pp. 551-565
    • Beltzner, C.C.1    Pollard, T.D.2
  • 3
    • 0032566659 scopus 로고    scopus 로고
    • Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin
    • Blanchoin L., and Pollard T.D. 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
  • 4
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments
    • Blanchoin L., and Pollard T.D. Mechanism of interaction of Acanthamoeba actophorin (ADF/cofilin) with actin filaments. J. Biol. Chem. 274 (1999) 15538-15546
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 5
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin
    • Blanchoin L., and Pollard T.D. Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin. Biochemistry 41 (2002) 597-602
    • (2002) Biochemistry , vol.41 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 7
    • 24944541377 scopus 로고    scopus 로고
    • Allostery of actin filaments: molecular dynamics simulations and coarse-grained analysis
    • Chu J.W., and Voth G.A. Allostery of actin filaments: molecular dynamics simulations and coarse-grained analysis. Proc. Natl. Acad. Sci. USA 102 (2005) 13111-13116
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13111-13116
    • Chu, J.W.1    Voth, G.A.2
  • 8
    • 26444593474 scopus 로고    scopus 로고
    • Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae
    • D'Agostino J.L., and Goode B.L. Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles for its nucleation-promoting factors in Saccharomyces cerevisiae. Genetics 171 (2005) 35-47
    • (2005) Genetics , vol.171 , pp. 35-47
    • D'Agostino, J.L.1    Goode, B.L.2
  • 9
    • 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
    • Dayel M.J., and Mullins R.D. 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
    • Dayel, M.J.1    Mullins, R.D.2
  • 10
    • 0035910044 scopus 로고    scopus 로고
    • Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments
    • Dayel M.J., Holleran E.A., and Mullins R.D. 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
  • 11
    • 0029825435 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species
    • De La Cruz E.M., and Pollard T.D. Kinetics and thermodynamics of phalloidin binding to actin filaments from three divergent species. Biochemistry 35 (1996) 14054-14061
    • (1996) Biochemistry , vol.35 , pp. 14054-14061
    • De La Cruz, E.M.1    Pollard, T.D.2
  • 12
    • 6344228185 scopus 로고    scopus 로고
    • Actin-binding proteins-a unifying hypothesis
    • Dominguez R. Actin-binding proteins-a unifying hypothesis. Trends Biochem. Sci. 29 (2004) 572-578
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 572-578
    • Dominguez, R.1
  • 15
    • 6344258806 scopus 로고    scopus 로고
    • Critical conformational changes in the Arp2/3 complex are induced by nucleotide and nucleation promoting factor
    • Goley E.D., Rodenbusch S.E., Martin A.C., and Welch M.D. 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
  • 16
    • 0141445972 scopus 로고    scopus 로고
    • Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics
    • Graceffa P., and Dominguez R. Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J. Biol. Chem. 278 (2003) 34172-34180
    • (2003) J. Biol. Chem. , vol.278 , pp. 34172-34180
    • Graceffa, P.1    Dominguez, R.2
  • 18
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins
    • Higgs H.N., and Pollard T.D. Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70 (2001) 649-676
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47 Pt 2 (1991) 110-119
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 21
    • 0034655949 scopus 로고    scopus 로고
    • The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework
    • Krebs W.G., and Gerstein M. The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework. Nucleic Acids Res. 28 (2000) 1665-1675
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1665-1675
    • Krebs, W.G.1    Gerstein, M.2
  • 22
    • 0027286199 scopus 로고
    • Selective binding of gelsolin to actin monomers containing ADP
    • Laham L.E., Lamb J.A., Allen P.G., and Janmey P.A. Selective binding of gelsolin to actin monomers containing ADP. J. Biol. Chem. 268 (1993) 14202-14207
    • (1993) J. Biol. Chem. , vol.268 , pp. 14202-14207
    • Laham, L.E.1    Lamb, J.A.2    Allen, P.G.3    Janmey, P.A.4
  • 23
    • 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 M.F., and Pantaloni D. Activation of Arp2/3 complex by Wiskott-Aldrich Syndrome protein is linked to enhanced binding of ATP to Arp2. J. Biol. Chem. 276 (2001) 46689-46692
    • (2001) J. Biol. Chem. , vol.276 , pp. 46689-46692
    • Le Clainche, C.1    Didry, D.2    Carlier, M.F.3    Pantaloni, D.4
  • 24
    • 0038313144 scopus 로고    scopus 로고
    • ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays
    • Le Clainche C., Pantaloni D., and Carlier M.F. ATP hydrolysis on actin-related protein 2/3 complex causes debranching of dendritic actin arrays. Proc. Natl. Acad. Sci. USA 100 (2003) 6337-6342
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6337-6342
    • Le Clainche, C.1    Pantaloni, D.2    Carlier, M.F.3
  • 26
    • 33746646463 scopus 로고    scopus 로고
    • Arp2/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation
    • Martin A.C., Welch M.D., and Drubin D.G. 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
  • 27
    • 0029661920 scopus 로고    scopus 로고
    • Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay
    • Melki R., Fievez S., and Carlier M.F. Continuous monitoring of Pi release following nucleotide hydrolysis in actin or tubulin assembly using 2-amino-6-mercapto-7-methylpurine ribonucleoside and purine-nucleoside phosphorylase as an enzyme-linked assay. Biochemistry 35 (1996) 12038-12045
    • (1996) Biochemistry , vol.35 , pp. 12038-12045
    • Melki, R.1    Fievez, S.2    Carlier, M.F.3
  • 28
    • 8144229871 scopus 로고    scopus 로고
    • Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
    • Nolen B.J., Littlefield R.S., and Pollard T.D. 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
  • 29
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., and Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 293 (2001) 708-711
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • in press
    • Pollard T.D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36 (2007) in press
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36
    • Pollard, T.D.1
  • 32
    • 0026666676 scopus 로고
    • Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin
    • Pollard T.D., Goldberg I., and Schwarz W.H. Nucleotide exchange, structure, and mechanical properties of filaments assembled from ATP-actin and ADP-actin. J. Biol. Chem. 267 (1992) 20339-20345
    • (1992) J. Biol. Chem. , vol.267 , pp. 20339-20345
    • Pollard, T.D.1    Goldberg, I.2    Schwarz, W.H.3
  • 34
    • 33846020951 scopus 로고    scopus 로고
    • Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states
    • Rould M.A., Wan Q., Joel P.B., Lowey S., and Trybus K.M. Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J. Biol. Chem. 281 (2006) 31909-31919
    • (2006) J. Biol. Chem. , vol.281 , pp. 31909-31919
    • Rould, M.A.1    Wan, Q.2    Joel, P.B.3    Lowey, S.4    Trybus, K.M.5
  • 35
    • 0033515062 scopus 로고    scopus 로고
    • Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics
    • Selden L.A., Kinosian H.J., Estes J.E., and Gershman L.C. Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics. Biochemistry 38 (1999) 2769-2778
    • (1999) Biochemistry , vol.38 , pp. 2769-2778
    • Selden, L.A.1    Kinosian, H.J.2    Estes, J.E.3    Gershman, L.C.4
  • 36
    • 0027523454 scopus 로고
    • Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion
    • Strzelecka-Golaszewska H., Moraczewska J., Khaitlina S.Y., and Mossakowska M. Localization of the tightly bound divalent-cation-dependent and nucleotide-dependent conformation changes in G-actin using limited proteolytic digestion. Eur. J. Biochem. 211 (1993) 731-742
    • (1993) Eur. J. Biochem. , vol.211 , pp. 731-742
    • Strzelecka-Golaszewska, H.1    Moraczewska, J.2    Khaitlina, S.Y.3    Mossakowska, M.4
  • 38
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks S.M., and McKay D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270 (1995) 2251-2257
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 39
    • 0033136019 scopus 로고    scopus 로고
    • Investigating a back door mechanism of actin phosphate release by steered molecular dynamics
    • Wriggers W., and Schulten K. Investigating a back door mechanism of actin phosphate release by steered molecular dynamics. Proteins 35 (1999) 262-273
    • (1999) Proteins , vol.35 , pp. 262-273
    • Wriggers, W.1    Schulten, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.