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Volumn 401, Issue 6756, 1999, Pages 926-929

Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; PROTEIN TYROSINE KINASE;

EID: 0033613455     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/44860     Document Type: Article
Times cited : (364)

References (27)
  • 1
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi, S. & Cossart, P. Intracellular pathogens and the actin cytoskeleton. Annu. Rev. Cell Dev. Biol. 14, 137-166 (1998).
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 137-166
    • Dramsi, S.1    Cossart, P.2
  • 2
    • 0030964241 scopus 로고    scopus 로고
    • Exploitation of mammalian host cell functions by bacterial pathogens
    • Finlay, B. B. & Cossart, P. Exploitation of mammalian host cell functions by bacterial pathogens. Science 276, 718-725 (1997).
    • (1997) Science , vol.276 , pp. 718-725
    • Finlay, B.B.1    Cossart, P.2
  • 3
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M. D., Iwamatsu, A. & Mitchison, T. J. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265-269 (1997).
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 4
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch, M. D., Rosenblatt, J., Skole, J., Portnoy, D. A. & Mitchison, T. J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281, 105-108 (1998).
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skole, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 5
    • 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
    • Mullins, D. R., Heuser, J. A. & Pollard, T. D. 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, 6181-6186 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, D.R.1    Heuser, J.A.2    Pollard, T.D.3
  • 6
    • 0028866712 scopus 로고
    • Actin-based motility of vaccinia virus
    • Cudmore, S., Cossart, P., Griffiths, G. & Way, M. Actin-based motility of vaccinia virus. Nature 378, 636-638 (1995).
    • (1995) Nature , vol.378 , pp. 636-638
    • Cudmore, S.1    Cossart, P.2    Griffiths, G.3    Way, M.4
  • 7
    • 0033611554 scopus 로고    scopus 로고
    • Tyrosine phosphorylation is required for actin based motility of vaccinia but not Listeria or Shigella
    • Frischknecht, F. et al. Tyrosine phosphorylation is required for actin based motility of vaccinia but not Listeria or Shigella. Curr. Biol. 9, 89-92 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 89-92
    • Frischknecht, F.1
  • 8
    • 0032213509 scopus 로고    scopus 로고
    • The Nck SH2/SH3 adaptor protein: A regulator of multiple intracellular signal transduction events
    • McCarty, J. H. The Nck SH2/SH3 adaptor protein: a regulator of multiple intracellular signal transduction events. BioEssays 20, 913-921 (1998).
    • (1998) BioEssays , vol.20 , pp. 913-921
    • McCarty, J.H.1
  • 9
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., Minura, K. & Takenawa, T. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326-5335 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5326-5335
    • Miki, H.1    Minura, K.2    Takenawa, T.3
  • 10
    • 0027419589 scopus 로고
    • Cortactin, an 80/85-kilodalton pp60sc substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • Wu, H. & Parsons, J. T. Cortactin, an 80/85-kilodalton pp60sc substrate, is a filamentous actin-binding protein enriched in the cell cortex. J. Cell Biol. 120, 1417-1426 (1993).
    • (1993) J. Cell Biol. , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 11
    • 0029005239 scopus 로고
    • Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp60c-src-mediated signalling pathway
    • Dehio, C., Prevost, M. C. & Sansonetti, P. J. Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp60c-src-mediated signalling pathway. EMBO J. 14, 2471-2482 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2471-2482
    • Dehio, C.1    Prevost, M.C.2    Sansonetti, P.J.3
  • 12
    • 0031806239 scopus 로고    scopus 로고
    • Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion
    • Sanderson, C. M., Frischknecht, F., Way, M., Hollinshead, M. & Smith, G. L. Roles of vaccinia virus EEV-specific proteins in intracellular actin tail formation and low pH-induced cell-cell fusion. J. Gen. Virol. 79, 1415-1425 (1998).
    • (1998) J. Gen. Virol. , vol.79 , pp. 1415-1425
    • Sanderson, C.M.1    Frischknecht, F.2    Way, M.3    Hollinshead, M.4    Smith, G.L.5
  • 13
    • 0345471829 scopus 로고    scopus 로고
    • Interactions between vaccinia virus IEV membrane proteins and their roles in IEV assembly and actin tail formation
    • Röttger, S., Frischknecht, F., Reckmann, I., Smith, G. L. & Way, M. Interactions between vaccinia virus IEV membrane proteins and their roles in IEV assembly and actin tail formation. J. Virol. 73, 2863-2875 (1999).
    • (1999) J. Virol. , vol.73 , pp. 2863-2875
    • Röttger, S.1    Frischknecht, F.2    Reckmann, I.3    Smith, G.L.4    Way, M.5
  • 14
    • 0032565358 scopus 로고    scopus 로고
    • Role for the vaccinia virus A36R outer envelope protein in the formation of virus-tipped actin-containing microvilli and cell-to-cell virus spread
    • Wolffe, E. J., Weisberg, A. S. & Moss, B. Role for the vaccinia virus A36R outer envelope protein in the formation of virus-tipped actin-containing microvilli and cell-to-cell virus spread. Virology 25, 20-26 (1998).
    • (1998) Virology , vol.25 , pp. 20-26
    • Wolffe, E.J.1    Weisberg, A.S.2    Moss, B.3
  • 15
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Songyang, Z. & Cantley, L. C. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem. Sci. 20, 470-475 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 16
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and src family selective tyrosine kinase inhibitor
    • Hanke, J. H. et al. Discovery of a novel, potent, and src family selective tyrosine kinase inhibitor. J. Biol. Chem. 271, 695-701 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 695-701
    • Hanke, J.H.1
  • 17
    • 0029126878 scopus 로고
    • Wiskott-Aldrich syndrome protein physically associates with Nck through Src3 homology domains
    • Rivero-Lezcano, O. M. & Marcilla, A., Sameshima, J. H. & Robbins, K. C. Wiskott-Aldrich syndrome protein physically associates with Nck through Src3 homology domains. Mol. Cell. Biol 15, 5725-5731 (1995).
    • (1995) Mol. Cell. Biol , vol.15 , pp. 5725-5731
    • Rivero-Lezcano, O.M.1    Marcilla, A.2    Sameshima, J.H.3    Robbins, K.C.4
  • 18
    • 0033012399 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein (WASP): Roles in signalling and cytoskeletal organization
    • Snapper, S. B. & Rosen, F. S. The Wiskott-Aldrich syndrome protein (WASP): roles in signalling and cytoskeletal organization. Annu. Rev. Immunol. 17, 905-929 (1999).
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 905-929
    • Snapper, S.B.1    Rosen, F.S.2
  • 19
    • 0032585538 scopus 로고    scopus 로고
    • Scarl and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M. & Insall, R. H. Scarl and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8, 1347-1356 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 20
    • 0033616763 scopus 로고    scopus 로고
    • Scar, a WASp-related protein, activates dendritic nucleation of actin filaments by the Arp2/3 complex
    • Machesky, L. M. et al. Scar, a WASp-related protein, activates dendritic nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA 96, 3739-3744 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 3739-3744
    • Machesky, L.M.1
  • 21
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R. et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231 (1999).
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1
  • 22
    • 0031906414 scopus 로고    scopus 로고
    • Virus-induced cell motility
    • Sanderson, C. M., Way, M. & Smith, G. L. Virus-induced cell motility. J. Virol. 72, 1235-1243 (1998).
    • (1998) J. Virol. , vol.72 , pp. 1235-1243
    • Sanderson, C.M.1    Way, M.2    Smith, G.L.3
  • 23
    • 0031775224 scopus 로고    scopus 로고
    • Vaccinia virus induces calcium-independent cell-matrix adhesion during the motile phase of infection
    • Sanderson, C. M. & Smith, G. L. Vaccinia virus induces calcium-independent cell-matrix adhesion during the motile phase of infection. J. Virol. 72, 9924-9933 (1998).
    • (1998) J. Virol. , vol.72 , pp. 9924-9933
    • Sanderson, C.M.1    Smith, G.L.2
  • 24
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni, S. et al. The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16, 7261-7271 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7261-7271
    • Gonfloni, S.1
  • 25
    • 0030862430 scopus 로고    scopus 로고
    • Compact, synthetic, vaccinia virus early/late promoter for protein expression
    • Chakrabarti, S., Sisler, J. R. & Moss, B. Compact, synthetic, vaccinia virus early/late promoter for protein expression. Biotechniques 23, 1094-1097 (1997).
    • (1997) Biotechniques , vol.23 , pp. 1094-1097
    • Chakrabarti, S.1    Sisler, J.R.2    Moss, B.3
  • 26
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley, A., Arnheim, N., Toney, M. D., Cortopassi, G. & Galas, D. J. A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res. 17, 6545-6551 (1989).
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 27
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domain of gelsolin and alpha-actinin: Implications for the requirements of severing and capping
    • Way, M., Pope, B. & Weeds, A. G. Evidence for functional homology in the F-actin binding domain of gelsolin and alpha-actinin: implications for the requirements of severing and capping. J. Cell Biol. 119, 835-842 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3


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