메뉴 건너뛰기




Volumn 14, Issue 2, 2006, Pages 257-263

Structure of the autoinhibitory switch in formin mDia1

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN FORMIN; RHO FACTOR; UNCLASSIFIED DRUG;

EID: 32044470440     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.12.003     Document Type: Article
Times cited : (87)

References (35)
  • 1
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoregulatory domain
    • A.S. Alberts Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoregulatory domain J. Biol. Chem. 276 2001 2824 2830
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 3
    • 0033607682 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility. Role of ADF/cofilin
    • M.F. Carlier, F. Ressad, and D. Pantaloni Control of actin dynamics in cell motility. Role of ADF/cofilin J. Biol. Chem. 274 1999 33827 33830
    • (1999) J. Biol. Chem. , vol.274 , pp. 33827-33830
    • Carlier, M.F.1    Ressad, F.2    Pantaloni, D.3
  • 4
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • D.H. Castrillon, and S.A. Wasserman Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene Development 120 1994 3367 3377
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 776
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-776
  • 6
    • 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
    • F. Chang, D. Drubin, and P. Nurse 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 1997 169 182
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 9
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • M. Evangelista, S. Zigmond, and C. Boone Formins: signaling effectors for assembly and polarization of actin filaments J. Cell Sci. 116 2003 2603 2611
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 10
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: A domain-based approach
    • H.N. Higgs Formin proteins: a domain-based approach Trends Biochem. Sci. 30 2005 342 353
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 11
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • H.N. Higgs, and K.J. Peterson Phylogenetic analysis of the formin homology 2 domain Mol. Biol. Cell 16 2005 1 13
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 12
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • H. Imamura, K. Tanaka, T. Hihara, M. Umikawa, T. Kamei, K. Takahashi, T. Sasaki, and Y. Takai Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae EMBO J. 16 1997 2745 2755
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 14
    • 0036223236 scopus 로고    scopus 로고
    • P21-activated kinases: Three more join the Pak
    • Z.M. Jaffer, and J. Chernoff P21-activated kinases: three more join the Pak Int. J. Biochem. Cell Biol. 34 2002 713 717
    • (2002) Int. J. Biochem. Cell Biol. , vol.34 , pp. 713-717
    • Jaffer, Z.M.1    Chernoff, J.2
  • 15
    • 0030841587 scopus 로고    scopus 로고
    • Electron-density map interpretation
    • T. Jones, and M. Kjeldgaard Electron-density map interpretation Methods Enzymol. 277 1997 173 208
    • (1997) Methods Enzymol. , vol.277 , pp. 173-208
    • Jones, T.1    Kjeldgaard, M.2
  • 16
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • W. Kabsch Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants J. Appl. Crystallogr. 26 1993 795 800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 17
    • 0030852350 scopus 로고    scopus 로고
    • Automated refinement for protein crystallography
    • V.S. Lamzin, and K.S. Wilson Automated refinement for protein crystallography Methods Enzymol. 277 1997 269 305
    • (1997) Methods Enzymol. , vol.277 , pp. 269-305
    • Lamzin, V.S.1    Wilson, K.S.2
  • 18
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • M. Lei, W. Lu, W. Meng, M.C. Parrini, M.J. Eck, B.J. Mayer, and S.C. Harrrison Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch Cell 102 2000 387 397
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrrison, S.C.7
  • 19
    • 18944386711 scopus 로고    scopus 로고
    • The active conformation of the PAK1 kinase domain
    • M. Lei, M.A. Robinson, and S.C. Harrison The active conformation of the PAK1 kinase domain Structure 13 2005 769 778
    • (2005) Structure , vol.13 , pp. 769-778
    • Lei, M.1    Robinson, M.A.2    Harrison, S.C.3
  • 20
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
    • F. Li, and H.N. Higgs Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1 J. Biol. Chem. 280 2005 6986 6992
    • (2005) J. Biol. Chem. , vol.280 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 22
    • 0032784388 scopus 로고    scopus 로고
    • Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells
    • K. Nakano, K. Takahashi, A. Kodama, A. Mammoto, H. Shiozaki, M. Monden, and Y. Takai Distinct actions and cooperative roles of ROCK and mDia in Rho small G protein-induced reorganization of the actin cytoskeleton in Madin-Darby canine kidney cells Mol. Biol. Cell 10 1999 2481 2491
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2481-2491
    • Nakano, K.1    Takahashi, K.2    Kodama, A.3    Mammoto, A.4    Shiozaki, H.5    Monden, M.6    Takai, Y.7
  • 23
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • T. Otomo, C. Otomo, D.R. Tomchick, M. Machius, and M.K. Rosen Structural basis of Rho GTPase-mediated activation of the formin mDia1 Mol. Cell 18 2005 273 281
    • (2005) Mol. Cell , vol.18 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    MacHius, M.4    Rosen, M.K.5
  • 24
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • T. Otomo, D.R. Tomchick, C. Otomo, S.C. Panchal, M. Machius, and M.K. Rosen Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain Nature 433 2005 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
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor 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
  • 26
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • A.F. Palazzo, T.A. Cook, A.S. Alberts, and G.G. Gundersen mDia mediates Rho-regulated formation and orientation of stable microtubules Nat. Cell Biol. 3 2001 723 729
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 27
    • 0036158988 scopus 로고    scopus 로고
    • Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1
    • M.C. Parrini, M. Lei, S.C. Harrison, and B.J. Mayer Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1 Mol. Cell 9 2002 73 83
    • (2002) Mol. Cell , vol.9 , pp. 73-83
    • Parrini, M.C.1    Lei, M.2    Harrison, S.C.3    Mayer, B.J.4
  • 29
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • R. Rose, M. Weyand, M. Lammers, T. Ishizaki, M.R. Ahmadian, and A. Wittinghofer Structural and mechanistic insights into the interaction between Rho and mammalian Dia Nature 435 2005 513 518
    • (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
  • 30
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • I. Sagot, S.K. Klee, and D. Pellman Yeast formins regulate cell polarity by controlling the assembly of actin cables Nat. Cell Biol. 4 2002 42 50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 31
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of Diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • A. Shimada, M. Nyitrai, I.R. Vetter, D. Kuhlmann, B. Bugyi, S. Narumiya, M.A. Geeves, and A. Wittinghofer The core FH2 domain of Diaphanous-related formins is an elongated actin binding protein that inhibits polymerization Mol. Cell 13 2004 511 522
    • (2004) Mol. Cell , vol.13 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumiya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 32
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • B.J. Wallar, and A.S. Alberts The formins: active scaffolds that remodel the cytoskeleton Trends Cell Biol. 13 2003 435 446
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 34
    • 0034649632 scopus 로고    scopus 로고
    • Actin dynamics: Assembly and disassembly of actin networks
    • M.A. Wear, D.A. Schafer, and J.A. Cooper Actin dynamics: assembly and disassembly of actin networks Curr. Biol. 10 2000 R891 R895
    • (2000) Curr. Biol. , vol.10
    • Wear, M.A.1    Schafer, D.A.2    Cooper, J.A.3
  • 35
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture
    • Y. Xu, J.B. Moseley, I. Sagot, F. Poy, D. Pellman, B.L. Goode, and M.J. Eck Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture Cell 116 2004 711 723
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.