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Volumn 3, Issue 6, 2013, Pages 1910-1920

Structural Basis of Actin Filament Nucleation by Tandem W Domains

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL PROTEIN; CORDON BLEU PROTEIN; UNCLASSIFIED DRUG;

EID: 84879798622     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.04.028     Document Type: Article
Times cited : (20)

References (64)
  • 2
    • 33644835262 scopus 로고    scopus 로고
    • The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins
    • Aguda A.H., Xue B., Irobi E., Préat T., Robinson R.C. The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure 2006, 14:469-476.
    • (2006) Structure , vol.14 , pp. 469-476
    • Aguda, A.H.1    Xue, B.2    Irobi, E.3    Préat, T.4    Robinson, R.C.5
  • 5
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone K.G., Welch M.D. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 2010, 11:237-251.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 6
    • 80052083395 scopus 로고    scopus 로고
    • Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu
    • Carlier M.F., Husson C., Renault L., Didry D. Control of actin assembly by the WH2 domains and their multifunctional tandem repeats in Spire and Cordon-Bleu. Int. Rev. Cell Mol. Biol. 2011, 290:55-85.
    • (2011) Int. Rev. Cell Mol. Biol. , vol.290 , pp. 55-85
    • Carlier, M.F.1    Husson, C.2    Renault, L.3    Didry, D.4
  • 8
    • 34547762177 scopus 로고    scopus 로고
    • Normal-mode refinement of anisotropic thermal parameters for potassium channel KcsA at 3.2 A crystallographic resolution
    • Chen X., Poon B.K., Dousis A., Wang Q., Ma J. Normal-mode refinement of anisotropic thermal parameters for potassium channel KcsA at 3.2 A crystallographic resolution. Structure 2007, 15:955-962.
    • (2007) Structure , vol.15 , pp. 955-962
    • Chen, X.1    Poon, B.K.2    Dousis, A.3    Wang, Q.4    Ma, J.5
  • 9
    • 84858967947 scopus 로고    scopus 로고
    • Multiple forms of Spire-actin complexes and their functional consequences
    • Chen C.K., Sawaya M.R., Phillips M.L., Reisler E., Quinlan M.E. Multiple forms of Spire-actin complexes and their functional consequences. J.Biol. Chem. 2012, 287:10684-10692.
    • (2012) J.Biol. Chem. , vol.287 , pp. 10684-10692
    • Chen, C.K.1    Sawaya, M.R.2    Phillips, M.L.3    Reisler, E.4    Quinlan, M.E.5
  • 10
    • 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. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 2005, 102:16644-16649.
    • (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
  • 11
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: mechanisms and interplay
    • Chesarone M.A., Goode B.L. Actin nucleation and elongation factors: mechanisms and interplay. Curr. Opin. Cell Biol. 2009, 21:28-37.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 12
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone M.A., DuPage A.G., Goode B.L. Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat. Rev. Mol. Cell Biol. 2010, 11:62-74.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 13
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra E.S., Higgs H.N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 2007, 9:1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 14
    • 0030575783 scopus 로고    scopus 로고
    • The structure of an open state of beta-actin at 2.65 A resolution
    • Chik J.K., Lindberg U., Schutt C.E. The structure of an open state of beta-actin at 2.65 A resolution. J.Mol. Biol. 1996, 263:607-623.
    • (1996) J.Mol. Biol. , vol.263 , pp. 607-623
    • Chik, J.K.1    Lindberg, U.2    Schutt, C.E.3
  • 15
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763. Collaborative Computational Project, Number 4.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 17
    • 80455168204 scopus 로고    scopus 로고
    • Nuclear actin and myosins: life without filaments
    • de Lanerolle P., Serebryannyy L. Nuclear actin and myosins: life without filaments. Nat. Cell Biol. 2011, 13:1282-1288.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1282-1288
    • de Lanerolle, P.1    Serebryannyy, L.2
  • 19
    • 6344228185 scopus 로고    scopus 로고
    • Actin-binding proteins-a unifying hypothesis
    • Dominguez R. Actin-binding proteins-a unifying hypothesis. Trends Biochem. Sci. 2004, 29:572-578.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 572-578
    • Dominguez, R.1
  • 20
    • 35348969696 scopus 로고    scopus 로고
    • The beta-thymosin/WH2 fold: multifunctionality and structure
    • Dominguez R. The beta-thymosin/WH2 fold: multifunctionality and structure. Ann. N Y Acad. Sci. 2007, 1112:86-94.
    • (2007) Ann. N Y Acad. Sci. , vol.1112 , pp. 86-94
    • Dominguez, R.1
  • 23
    • 82655181326 scopus 로고    scopus 로고
    • The actin nucleation factor JMY is a negative regulator of neuritogenesis
    • Firat-Karalar E.N., Hsiue P.P., Welch M.D. The actin nucleation factor JMY is a negative regulator of neuritogenesis. Mol. Biol. Cell 2011, 22:4563-4574.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4563-4574
    • Firat-Karalar, E.N.1    Hsiue, P.P.2    Welch, M.D.3
  • 24
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T., Iwane A.H., Yanagida T., Namba K. Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 2010, 467:724-728.
    • (2010) Nature , vol.467 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 25
    • 0029046580 scopus 로고
    • Characterization of a gene trap insertion into a novel gene, cordon-bleu, expressed in axial structures of the gastrulating mouse embryo
    • Gasca S., Hill D.P., Klingensmith J., Rossant J. Characterization of a gene trap insertion into a novel gene, cordon-bleu, expressed in axial structures of the gastrulating mouse embryo. Dev. Genet. 1995, 17:141-154.
    • (1995) Dev. Genet. , vol.17 , pp. 141-154
    • Gasca, S.1    Hill, D.P.2    Klingensmith, J.3    Rossant, J.4
  • 26
    • 0141445972 scopus 로고    scopus 로고
    • Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics
    • Graceffa P., Dominguez R. Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J.Biol. Chem. 2003, 278:34172-34180.
    • (2003) J.Biol. Chem. , vol.278 , pp. 34172-34180
    • Graceffa, P.1    Dominguez, R.2
  • 30
    • 79960930017 scopus 로고    scopus 로고
    • Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly
    • Husson C., Renault L., Didry D., Pantaloni D., Carlier M.F. Cordon-Bleu uses WH2 domains as multifunctional dynamizers of actin filament assembly. Mol. Cell 2011, 43:464-477.
    • (2011) Mol. Cell , vol.43 , pp. 464-477
    • Husson, C.1    Renault, L.2    Didry, D.3    Pantaloni, D.4    Carlier, M.F.5
  • 32
    • 51049096605 scopus 로고    scopus 로고
    • Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants
    • Iwasa M., Maeda K., Narita A., Maéda Y., Oda T. Dual roles of Gln137 of actin revealed by recombinant human cardiac muscle alpha-actin mutants. J.Biol. Chem. 2008, 283:21045-21053.
    • (2008) J.Biol. Chem. , vol.283 , pp. 21045-21053
    • Iwasa, M.1    Maeda, K.2    Narita, A.3    Maéda, Y.4    Oda, T.5
  • 33
    • 4444344286 scopus 로고    scopus 로고
    • Expression of a nonpolymerizable actin mutant in Sf9 cells
    • Joel P.B., Fagnant P.M., Trybus K.M. Expression of a nonpolymerizable actin mutant in Sf9 cells. Biochemistry 2004, 43:11554-11559.
    • (2004) Biochemistry , vol.43 , pp. 11554-11559
    • Joel, P.B.1    Fagnant, P.M.2    Trybus, K.M.3
  • 34
    • 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., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 1991, 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 77957793677 scopus 로고    scopus 로고
    • Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release
    • Murakami K., Yasunaga T., Noguchi T.Q., Gomibuchi Y., Ngo K.X., Uyeda T.Q., Wakabayashi T. Structural basis for actin assembly, activation of ATP hydrolysis, and delayed phosphate release. Cell 2010, 143:275-287.
    • (2010) Cell , vol.143 , pp. 275-287
    • Murakami, K.1    Yasunaga, T.2    Noguchi, T.Q.3    Gomibuchi, Y.4    Ngo, K.X.5    Uyeda, T.Q.6    Wakabayashi, T.7
  • 38
    • 34948868986 scopus 로고    scopus 로고
    • A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant
    • Noguchi T.Q., Kanzaki N., Ueno H., Hirose K., Uyeda T.Q. A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant. J.Biol. Chem. 2007, 282:27721-27727.
    • (2007) J.Biol. Chem. , vol.282 , pp. 27721-27727
    • Noguchi, T.Q.1    Kanzaki, N.2    Ueno, H.3    Hirose, K.4    Uyeda, T.Q.5
  • 39
    • 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., Pollard T.D. Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proc. Natl. Acad. Sci. USA 2004, 101:15627-15632.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15627-15632
    • Nolen, B.J.1    Littlefield, R.S.2    Pollard, T.D.3
  • 40
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maéda Y., Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009, 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 41
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • Otomo T., Tomchick D.R., Otomo C., Panchal S.C., Machius M., Rosen M.K. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 2005, 433:488-494.
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 42
    • 0035958757 scopus 로고    scopus 로고
    • The crystal structure of uncomplexed actin in the ADP state
    • Otterbein L.R., Graceffa P., Dominguez R. The crystal structure of uncomplexed actin in the ADP state. Science 2001, 293:708-711.
    • (2001) Science , vol.293 , pp. 708-711
    • Otterbein, L.R.1    Graceffa, P.2    Dominguez, R.3
  • 43
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: a small, versatile adapter for actin monomers
    • Paunola E., Mattila P.K., Lappalainen P. WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 2002, 513:92-97.
    • (2002) FEBS Lett. , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 44
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard T.D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:451-477.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 45
    • 34249944597 scopus 로고    scopus 로고
    • Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution
    • Poon B.K., Chen X., Lu M., Vyas N.K., Quiocho F.A., Wang Q., Ma J. Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution. Proc. Natl. Acad. Sci. USA 2007, 104:7869-7874.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7869-7874
    • Poon, B.K.1    Chen, X.2    Lu, M.3    Vyas, N.K.4    Quiocho, F.A.5    Wang, Q.6    Ma, J.7
  • 46
    • 0033212804 scopus 로고    scopus 로고
    • The Rossmann Fourier autoindexing algorithm in MOSFLM
    • Powell H.R. The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 1999, 55:1690-1695.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1690-1695
    • Powell, H.R.1
  • 47
    • 66349133039 scopus 로고    scopus 로고
    • New players in actin polymerization-WH2-domain-containing actin nucleators
    • Qualmann B., Kessels M.M. New players in actin polymerization-WH2-domain-containing actin nucleators. Trends Cell Biol. 2009, 19:276-285.
    • (2009) Trends Cell Biol. , vol.19 , pp. 276-285
    • Qualmann, B.1    Kessels, M.M.2
  • 49
    • 78651237576 scopus 로고    scopus 로고
    • The actin nucleator Cordon-bleu is required for development of motile cilia in zebrafish
    • Ravanelli A.M., Klingensmith J. The actin nucleator Cordon-bleu is required for development of motile cilia in zebrafish. Dev. Biol. 2011, 350:101-111.
    • (2011) Dev. Biol. , vol.350 , pp. 101-111
    • Ravanelli, A.M.1    Klingensmith, J.2
  • 51
    • 77957267062 scopus 로고    scopus 로고
    • Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation
    • Rebowski G., Namgoong S., Boczkowska M., Leavis P.C., Navaza J., Dominguez R. Structure of a longitudinal actin dimer assembled by tandem w domains: implications for actin filament nucleation. J.Mol. Biol. 2010, 403:11-23.
    • (2010) J.Mol. Biol. , vol.403 , pp. 11-23
    • Rebowski, G.1    Namgoong, S.2    Boczkowska, M.3    Leavis, P.C.4    Navaza, J.5    Dominguez, R.6
  • 52
    • 37549005604 scopus 로고    scopus 로고
    • Actin structure and function: what we still do not understand
    • Reisler E., Egelman E.H. Actin structure and function: what we still do not understand. J.Biol. Chem. 2007, 282:36133-36137.
    • (2007) J.Biol. Chem. , vol.282 , pp. 36133-36137
    • Reisler, E.1    Egelman, E.H.2
  • 55
    • 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., Trybus K.M. Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J.Biol. Chem. 2006, 281:31909-31919.
    • (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
  • 57
    • 79961021014 scopus 로고    scopus 로고
    • The functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin I
    • Schwintzer L., Koch N., Ahuja R., Grimm J., Kessels M.M., Qualmann B. The functions of the actin nucleator Cobl in cellular morphogenesis critically depend on syndapin I. EMBO J. 2011, 30:3147-3159.
    • (2011) EMBO J. , vol.30 , pp. 3147-3159
    • Schwintzer, L.1    Koch, N.2    Ahuja, R.3    Grimm, J.4    Kessels, M.M.5    Qualmann, B.6
  • 60
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich J.A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J.Biol. Chem. 1971, 246:4866-4871.
    • (1971) J.Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 61
    • 79954471953 scopus 로고    scopus 로고
    • JMY is required for asymmetric division and cytokinesis in mouse oocytes
    • Sun S.C., Sun Q.Y., Kim N.H. JMY is required for asymmetric division and cytokinesis in mouse oocytes. Mol. Hum. Reprod. 2011, 17:296-304.
    • (2011) Mol. Hum. Reprod. , vol.17 , pp. 296-304
    • Sun, S.C.1    Sun, Q.Y.2    Kim, N.H.3
  • 62
    • 0030588963 scopus 로고    scopus 로고
    • Overexpression of actin in AcMNPV-infected cells interferes with polyhedrin synthesis and polyhedra formation
    • Volkman L., Storm K., Aivazachvili V., Oppenheimer D. Overexpression of actin in AcMNPV-infected cells interferes with polyhedrin synthesis and polyhedra formation. Virology 1996, 225:369-376.
    • (1996) Virology , vol.225 , pp. 369-376
    • Volkman, L.1    Storm, K.2    Aivazachvili, V.3    Oppenheimer, D.4


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