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Volumn 11, Issue 10, 2009, Pages 1212-1218

The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ADAPTOR PROTEIN TUBA; BACTERIAL PROTEIN; INTERNALIN C; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; UNCLASSIFIED DRUG;

EID: 70349634308     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1964     Document Type: Article
Times cited : (148)

References (28)
  • 1
    • 13444301168 scopus 로고    scopus 로고
    • Actin-based motility of intracellular pathogens
    • Gouin, E., Welch, W. D. & Cossart, P. Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8, 35-45 (2005).
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 35-45
    • Gouin, E.1    Welch, W.D.2    Cossart, P.3
  • 2
    • 0142026447 scopus 로고    scopus 로고
    • Regulation of actin dynamics by WASP family proteins
    • Miki, H. & Takenawa, T. Regulation of actin dynamics by WASP family proteins. J. Biochem. 134, 309-313 (2003).
    • (2003) J. Biochem , vol.134 , pp. 309-313
    • Miki, H.1    Takenawa, T.2
  • 3
    • 33749548025 scopus 로고    scopus 로고
    • Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells
    • Otani, T., Ichii, T., Aono, S. & Takeichi, M. Cdc42 GEF Tuba regulates the junctional configuration of simple epithelial cells. J. Cell Biol. 175, 135-46 (2006).
    • (2006) J. Cell Biol , vol.175 , pp. 135-146
    • Otani, T.1    Ichii, T.2    Aono, S.3    Takeichi, M.4
  • 4
    • 0034934605 scopus 로고    scopus 로고
    • Listeria pathogenesis and molecular virulence determinants
    • Vazquez-Boland, J. A. et al. Listeria pathogenesis and molecular virulence determinants. Clin. Microbiol. Rev. 14, 584-640 (2001).
    • (2001) Clin. Microbiol. Rev , vol.14 , pp. 584-640
    • Vazquez-Boland, J.A.1
  • 5
    • 0033588919 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits normal host cell processes to spread from cell to cell
    • Robbins, J. R. et al. Listeria monocytogenes exploits normal host cell processes to spread from cell to cell. J. Cell Biol. 146 1333-1349 (1999).
    • (1999) J. Cell Biol , vol.146 , pp. 1333-1349
    • Robbins, J.R.1
  • 6
    • 0034843552 scopus 로고    scopus 로고
    • Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake
    • Monack, D. M. & Theriot, J. A. Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake. Cell. Microbiol. 3, 633-647 (2001).
    • (2001) Cell. Microbiol , vol.3 , pp. 633-647
    • Monack, D.M.1    Theriot, J.A.2
  • 7
    • 16844365885 scopus 로고    scopus 로고
    • Molecular perspective on tight-junction assembly and epithelial polarity
    • Miyoshi, J. & Takai, Y. Molecular perspective on tight-junction assembly and epithelial polarity. Adv. Drug Deliv. Rev. 57, 815-855 (2005).
    • (2005) Adv. Drug Deliv. Rev , vol.57 , pp. 815-855
    • Miyoshi, J.1    Takai, Y.2
  • 8
    • 0035368519 scopus 로고    scopus 로고
    • A transgenic model for Listeriosis: Role of internalin in crossing the intestinal barrier
    • Lecuit, M. et al. A transgenic model for Listeriosis: Role of internalin in crossing the intestinal barrier. Science 292, 1722-1725 (2001).
    • (2001) Science , vol.292 , pp. 1722-1725
    • Lecuit, M.1
  • 9
    • 0026755585 scopus 로고
    • Characterization of the enterocyte-like brush border cytoskeleton
    • Peterson, M. D. & Mooseker, M. S. Characterization of the enterocyte-like brush border cytoskeleton. J. Cell. Sci. 102 581-600 (1992).
    • (1992) J. Cell. Sci , vol.102 , pp. 581-600
    • Peterson, M.D.1    Mooseker, M.S.2
  • 10
    • 0025016446 scopus 로고
    • Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread
    • Sun, A. N., Camilli, A. & Portnoy, D. A. Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread. Infect. Immun. 58, 3770-3778 (1990).
    • (1990) Infect. Immun , vol.58 , pp. 3770-3778
    • Sun, A.N.1    Camilli, A.2    Portnoy, D.A.3
  • 11
    • 0029745347 scopus 로고    scopus 로고
    • A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins
    • Engelbrecht. F. et al. A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins. Mol. Microbiol. 21, 823-837 (1996).
    • (1996) Mol. Microbiol , vol.21 , pp. 823-837
    • Engelbrecht, F.1
  • 12
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have ovelapping roles in escape from a vacuole and cell-to-cell spread
    • Smith, G. A. et al. The two distinct phospholipases C of Listeria monocytogenes have ovelapping roles in escape from a vacuole and cell-to-cell spread. Infec. Immun. 63, 4231-4237 (1995).
    • (1995) Infec. Immun , vol.63 , pp. 4231-4237
    • Smith, G.A.1
  • 13
    • 0029807736 scopus 로고    scopus 로고
    • The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin
    • Smith, G. A., Theriot, J. & Portnoy, D. The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin. J. Cell Biol. 135, 647-660 (1996).
    • (1996) J. Cell Biol , vol.135 , pp. 647-660
    • Smith, G.A.1    Theriot, J.2    Portnoy, D.3
  • 14
    • 34247516852 scopus 로고    scopus 로고
    • ERM proteins in epithelial cell organization and functions
    • Fievet, B., Louvard, D. & Arpin, M. ERM proteins in epithelial cell organization and functions. Biochim. Biophys. Acta. 1773, 653-660 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 653-660
    • Fievet, B.1    Louvard, D.2    Arpin, M.3
  • 15
    • 17144399487 scopus 로고    scopus 로고
    • Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell
    • Pust, S., Morrison, H., Wehland, J., Sechi, A. S. & Herrlich, P. Listeria monocytogenes exploits ERM protein functions to efficiently spread from cell to cell. EMBO J. 24, 1287-1300 (2005).
    • (2005) EMBO J , vol.24 , pp. 1287-1300
    • Pust, S.1    Morrison, H.2    Wehland, J.3    Sechi, A.S.4    Herrlich, P.5
  • 16
    • 0030908903 scopus 로고    scopus 로고
    • The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random
    • Sechi, A. S., Wehland, J. & Small, J. V. The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random. J. Cell Biol. 137, 155-167 (1997).
    • (1997) J. Cell Biol , vol.137 , pp. 155-167
    • Sechi, A.S.1    Wehland, J.2    Small, J.V.3
  • 17
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B. & Kajava, A. V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11, 725-732 (2001).
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 18
    • 34548491198 scopus 로고    scopus 로고
    • Internalins: A complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes
    • Bierne, H., Sabet, C., Personnic, N. & Cossart, P. Internalins: A complex family of leucine-rich repeat-containing proteins in Listeria monocytogenes. Microbes Infec. 9, 1156-66 (2007).
    • (2007) Microbes Infec , vol.9 , pp. 1156-1166
    • Bierne, H.1    Sabet, C.2    Personnic, N.3    Cossart, P.4
  • 19
    • 1542677037 scopus 로고    scopus 로고
    • Tuba, a novel protein containing Bin-Amphysin-Rvs and Dbl homology domains, links Dynamin to regulation of the actin cytoskeleton
    • Salazar, M. A. et al. Tuba, a novel protein containing Bin-Amphysin-Rvs and Dbl homology domains, links Dynamin to regulation of the actin cytoskeleton. J. Biol. Chem. 278, 49031-49043 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 49031-49043
    • Salazar, M.A.1
  • 20
    • 33746863655 scopus 로고    scopus 로고
    • Tuba stimulates N-WASP-dependent actin assembly
    • Kovacs, E. M., Makar, R. S. & Gertler, F. B. Tuba stimulates N-WASP-dependent actin assembly. J. Cell Sci. 119, 2715-2726 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 2715-2726
    • Kovacs, E.M.1    Makar, R.S.2    Gertler, F.B.3
  • 21
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction
    • Li, S. S. C. Specificity and versatility of SH3 and other proline-recognition domains: Structural basis and implications for cellular signal transduction. Biochem. J. 390, 641-653 (2005).
    • (2005) Biochem. J , vol.390 , pp. 641-653
    • Li, S.S.C.1
  • 22
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor
    • Straight, A. F. et al. Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor. Science 299, 1743-1747 (2003).
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1
  • 23
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • Riento, K. & Ridley, A. J. Rocks: Multifunctional kinases in cell behaviour. Nature Rev. Mol. Cell Biol. 4, 456-456 (2003).
    • (2003) Nature Rev. Mol. Cell Biol , vol.4 , pp. 456-456
    • Riento, K.1    Ridley, A.J.2
  • 24
    • 0033672942 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions IV. Regulation of tight junctions by extracellular stimuli: Nutrients, cytokines, and immune cells
    • Nusrat, A., Turner, J. R. & Madara, J. L. Molecular physiology and pathophysiology of tight junctions IV. Regulation of tight junctions by extracellular stimuli: Nutrients, cytokines, and immune cells. Am. J. Physiol. Gastrointest. Liver Physiol. 279, G851-G857 (2000).
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol , vol.279
    • Nusrat, A.1    Turner, J.R.2    Madara, J.L.3
  • 25
    • 0025785109 scopus 로고
    • Gene disruption by plasmid integration in Listeria monocytogenes: Insertional inactivation of the listeriolysin determinant lisA
    • Wuenscher, M. D., Kohler, S., Goebel, W. & Chakraborty, T. Gene disruption by plasmid integration in Listeria monocytogenes: insertional inactivation of the listeriolysin determinant lisA. Mol. Gen. Genet. 228, 177-182 (1991).
    • (1991) Mol. Gen. Genet , vol.228 , pp. 177-182
    • Wuenscher, M.D.1    Kohler, S.2    Goebel, W.3    Chakraborty, T.4
  • 26
    • 33847420373 scopus 로고    scopus 로고
    • Mechanism of actin network attachment to moving membranes: Barbed end capture by N-WASP WH2 domains
    • Co, C., Wong, D. T., Gierke, S., Chang, V. & Taunton, J. Mechanism of actin network attachment to moving membranes: Barbed end capture by N-WASP WH2 domains. Cell 128, 901-913 (2007).
    • (2007) Cell , vol.128 , pp. 901-913
    • Co, C.1    Wong, D.T.2    Gierke, S.3    Chang, V.4    Taunton, J.5
  • 27
    • 14044257839 scopus 로고    scopus 로고
    • Host adaptor proteins Gab1 and CrkII promote InlB-dependent entry of Listeria monocytogenes
    • Sun, H. et al. Host adaptor proteins Gab1 and CrkII promote InlB-dependent entry of Listeria monocytogenes. Cell. Microbiol. 7, 443-457 (2005).
    • (2005) Cell. Microbiol , vol.7 , pp. 443-457
    • Sun, H.1
  • 28
    • 0141677821 scopus 로고    scopus 로고
    • Ena-VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility
    • Auerbuch, V., Loureiro, J. J., Gertler, F. B., Theriot, J. A. & Portnoy, D. A. Ena-VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility. Mol. Microbiol. 49, 1361-1375 (2003).
    • (2003) Mol. Microbiol , vol.49 , pp. 1361-1375
    • Auerbuch, V.1    Loureiro, J.J.2    Gertler, F.B.3    Theriot, J.A.4    Portnoy, D.A.5


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