메뉴 건너뛰기




Volumn 359, Issue 4, 2006, Pages 840-847

Cortactin Binding to F-actin Revealed by Electron Microscopy and 3D Reconstruction

Author keywords

actin; Arp2 3; cortactin; electron microscopy; WASP

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; CORTACTIN; F ACTIN;

EID: 33744832052     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.03.065     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., and Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112 (2003) 453-465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 4644342865 scopus 로고    scopus 로고
    • Regulation of WASP/WAVE proteins: making a long story short
    • Bompard G., and Caron E. Regulation of WASP/WAVE proteins: making a long story short. J. Cell Biol. 166 (2004) 957-962
    • (2004) J. Cell Biol. , vol.166 , pp. 957-962
    • Bompard, G.1    Caron, E.2
  • 3
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M., Derry J.M., Karlak B., Jiang S., Lemahieu V., McCormick F., et al. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84 (1996) 723-734
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6
  • 4
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky L.M., and Insall R.H. 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
  • 5
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno T., Liu J., Zhang P., Fan Y., Egile C., Li R., et al. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nature Cell Biol. 3 (2001) 259-266
    • (2001) Nature Cell Biol. , vol.3 , pp. 259-266
    • Uruno, T.1    Liu, J.2    Zhang, P.3    Fan, Y.4    Egile, C.5    Li, R.6
  • 7
    • 4344674527 scopus 로고    scopus 로고
    • Cortactin signaling and dynamic actin networks
    • Daly R.J. Cortactin signaling and dynamic actin networks. Biochem. J. 382 (2004) 13-25
    • (2004) Biochem. J. , vol.382 , pp. 13-25
    • Daly, R.J.1
  • 8
    • 16244370694 scopus 로고    scopus 로고
    • Cortactin: an Achilles' heel of the actin cytoskeleton targeted by pathogens
    • Selbach M., and Backert S. Cortactin: an Achilles' heel of the actin cytoskeleton targeted by pathogens. Trends Microbiol. 13 (2005) 181-189
    • (2005) Trends Microbiol. , vol.13 , pp. 181-189
    • Selbach, M.1    Backert, S.2
  • 9
    • 0035475450 scopus 로고    scopus 로고
    • Cortactin: coupling membrane dynamics to cortical actin assembly
    • Weed S.A., and Parsons J.T. Cortactin: coupling membrane dynamics to cortical actin assembly. Oncogene 20 (2001) 6418-6434
    • (2001) Oncogene , vol.20 , pp. 6418-6434
    • Weed, S.A.1    Parsons, J.T.2
  • 10
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu H., and Parsons J.T. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120 (1993) 1417-1426
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 11
    • 0035146636 scopus 로고    scopus 로고
    • Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
    • Marchand J.B., Kaiser D.A., Pollard T.D., and Higgs H.N. Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nature Cell Biol. 3 (2001) 76-82
    • (2001) Nature Cell Biol. , vol.3 , pp. 76-82
    • Marchand, J.B.1    Kaiser, D.A.2    Pollard, T.D.3    Higgs, H.N.4
  • 13
    • 0029890281 scopus 로고    scopus 로고
    • Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins
    • Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., and Kay B.K. Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. Nature Biotech. 14 (1996) 741-744
    • (1996) Nature Biotech. , vol.14 , pp. 741-744
    • Sparks, A.B.1    Hoffman, N.G.2    McConnell, S.J.3    Fowlkes, D.M.4    Kay, B.K.5
  • 14
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex
    • Weed S.A., Karginov A.V., Schafer D.A., Weaver A.M., Kinley A.W., Cooper J.A., and Parsons J.T. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J. Cell Biol. 151 (2000) 29-40
    • (2000) J. Cell Biol. , vol.151 , pp. 29-40
    • Weed, S.A.1    Karginov, A.V.2    Schafer, D.A.3    Weaver, A.M.4    Kinley, A.W.5    Cooper, J.A.6    Parsons, J.T.7
  • 15
    • 0036468250 scopus 로고    scopus 로고
    • Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts
    • Mizutani K., Miki H., He H., Maruta H., and Takenawa T. Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in src-transformed fibroblasts. Cancer Res. 62 (2002) 669-674
    • (2002) Cancer Res. , vol.62 , pp. 669-674
    • Mizutani, K.1    Miki, H.2    He, H.3    Maruta, H.4    Takenawa, T.5
  • 16
    • 2942594602 scopus 로고    scopus 로고
    • Erk/Src phosphorylation of cortactin acts as a switch on-switch off mechanism that controls its ability to activate N-WASP
    • Martinez-Quiles N., Ho H.Y., Kirschner M.W., Ramesh N., and Geha R.S. Erk/Src phosphorylation of cortactin acts as a switch on-switch off mechanism that controls its ability to activate N-WASP. Mol. Cell. Biol. 24 (2004) 5269-5280
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5269-5280
    • Martinez-Quiles, N.1    Ho, H.Y.2    Kirschner, M.W.3    Ramesh, N.4    Geha, R.S.5
  • 17
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by use of a directed mutation algorithm
    • Lorenz M., Popp D., and Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by use of a directed mutation algorithm. J. Mol. Biol. 234 (1993) 826-836
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 19
    • 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
  • 20
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function
    • McGough A., Pope B., Chui W., and Weeds A. 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    Chui, W.3    Weeds, A.4
  • 21
    • 27844455570 scopus 로고    scopus 로고
    • Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions
    • Egile C., Rouiller I., Xu X.P., Volkmann N., Li R., and Hanein D. Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions. PLoS Biol. 3 (2005) 1902-1909
    • (2005) PLoS Biol. , vol.3 , pp. 1902-1909
    • Egile, C.1    Rouiller, I.2    Xu, X.P.3    Volkmann, N.4    Li, R.5    Hanein, D.6
  • 22
    • 0035964794 scopus 로고    scopus 로고
    • Structure of Arp2/3 complex in its activated state and in actin filament branch junctions
    • Volkmann N., Amann K.J., Stoilova-McPhie S., Egile C., Winter D.C., Hazelwood L., et al. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 293 (2001) 2456-2459
    • (2001) Science , vol.293 , pp. 2456-2459
    • Volkmann, N.1    Amann, K.J.2    Stoilova-McPhie, S.3    Egile, C.4    Winter, D.C.5    Hazelwood, L.6
  • 23
    • 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., and 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. 242 (1971) 4866-4871
    • (1971) J. Biol. Chem. , vol.242 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 24
    • 0025308841 scopus 로고
    • Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments
    • Moody C., Lehman W., and Craig R. Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments. J. Muscle Res. Cell Motil. 11 (1990) 176-185
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 176-185
    • Moody, C.1    Lehman, W.2    Craig, R.3
  • 25
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments
    • Moore P.B., Huxley H.E., and DeRosier D.J. Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments. J. Mol. Biol. 50 (1970) 279-295
    • (1970) J. Mol. Biol. , vol.50 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    DeRosier, D.J.3
  • 26
    • 0022928662 scopus 로고
    • An algorithm for straightening images of curved filamentous structures
    • Egelman E.H. An algorithm for straightening images of curved filamentous structures. Ultramicroscopy 19 (1986) 367-374
    • (1986) Ultramicroscopy , vol.19 , pp. 367-374
    • Egelman, E.H.1
  • 27
    • 0030927201 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon
    • Hodgkinson J.L., Marston S.B., Craig R., Vibert P., and Lehman W. Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon. Biophys. J. 72 (1997) 2398-2404
    • (1997) Biophys. J. , vol.72 , pp. 2398-2404
    • Hodgkinson, J.L.1    Marston, S.B.2    Craig, R.3    Vibert, P.4    Lehman, W.5
  • 28
    • 0029916489 scopus 로고    scopus 로고
    • Image analysis of helical objects: the Brandeis helical package
    • Owen C., Morgan D.G., and DeRosier D.J. Image analysis of helical objects: the Brandeis helical package. J. Struct. Biol. 116 (1996) 167-175
    • (1996) J. Struct. Biol. , vol.116 , pp. 167-175
    • Owen, C.1    Morgan, D.G.2    DeRosier, D.J.3
  • 29
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 30
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
    • Milligan R.A., and Flicker P.F. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell. Biol. 105 (1987) 29-39
    • (1987) J. Cell. Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 31
    • 0023644892 scopus 로고
    • Three-dimensional structure of the frozen hydrated flagellar filament: the left-handed filament of Salmonella typhimurium
    • Trachtenberg S., and DeRosier D.J. Three-dimensional structure of the frozen hydrated flagellar filament: the left-handed filament of Salmonella typhimurium. J. Mol. Biol. 195 (1987) 581-601
    • (1987) J. Mol. Biol. , vol.195 , pp. 581-601
    • Trachtenberg, S.1    DeRosier, D.J.2
  • 32
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and 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 location of errors in these models. Acta Crystallog. sect. A 47 (1991) 110-119
    • (1991) Acta Crystallog. sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 33
    • 13844297588 scopus 로고    scopus 로고
    • Single particle analysis of relaxed and activated thin filaments
    • Pirani A., Xu C., Hatch V., Craig R., and Lehman W. Single particle analysis of relaxed and activated thin filaments. J. Mol. Biol. 346 (2005) 761-772
    • (2005) J. Mol. Biol. , vol.346 , pp. 761-772
    • Pirani, A.1    Xu, C.2    Hatch, V.3    Craig, R.4    Lehman, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.