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Volumn 14, Issue 2, 2012, Pages 226-238

The cooperative action of bacterial fibronectin-binding proteins and secreted proteins promote maximal Campylobacter jejuni invasion of host cells by stimulating membrane ruffling

Author keywords

[No Author keywords available]

Indexed keywords

CADF PROTEIN; DOCK180 PROTEIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; FIBRONECTIN BINDING PROTEIN; FLPA PROTEIN; FOCAL ADHESION KINASE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN; RAC1 PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84856048267     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2011.01714.x     Document Type: Article
Times cited : (89)

References (47)
  • 3
    • 13544252448 scopus 로고    scopus 로고
    • Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement
    • Beardsley, A., Fang, K., Mertz, H., Castranova, V., Friend, S., and Liu, J. (2005) Loss of caveolin-1 polarity impedes endothelial cell polarization and directional movement. J Biol Chem 280: 3541-3547.
    • (2005) J Biol Chem , vol.280 , pp. 3541-3547
    • Beardsley, A.1    Fang, K.2    Mertz, H.3    Castranova, V.4    Friend, S.5    Liu, J.6
  • 4
    • 0036265520 scopus 로고    scopus 로고
    • Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade
    • Buchsbaum, R.J., Connolly, B.A., and Feig, L.A. (2002) Interaction of Rac exchange factors Tiam1 and Ras-GRF1 with a scaffold for the p38 mitogen-activated protein kinase cascade. Mol Cell Biol 22: 4073-4085.
    • (2002) Mol Cell Biol , vol.22 , pp. 4073-4085
    • Buchsbaum, R.J.1    Connolly, B.A.2    Feig, L.A.3
  • 5
    • 79957464852 scopus 로고    scopus 로고
    • Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI
    • Buelow, D.R., Christensen, J.E., Neal-McKinney, J.M., and Konkel, M.E. (2011) Campylobacter jejuni survival within human epithelial cells is enhanced by the secreted protein CiaI. Mol Microbiol 80: 1296-1312.
    • (2011) Mol Microbiol , vol.80 , pp. 1296-1312
    • Buelow, D.R.1    Christensen, J.E.2    Neal-McKinney, J.M.3    Konkel, M.E.4
  • 6
    • 3042653012 scopus 로고    scopus 로고
    • Integrin regulation of epidermal growth factor (EGF) receptor and of EGF-dependent responses
    • Cabodi, S., Moro, L., Bergatto, E., Boeri Erba, E., Di Stefano, P., Turco, E., etal. (2004) Integrin regulation of epidermal growth factor (EGF) receptor and of EGF-dependent responses. Biochem Soc Trans 32: 438-442.
    • (2004) Biochem Soc Trans , vol.32 , pp. 438-442
    • Cabodi, S.1    Moro, L.2    Bergatto, E.3    Boeri Erba, E.4    Di Stefano, P.5    Turco, E.6
  • 7
    • 0033555070 scopus 로고    scopus 로고
    • Focal adhesion kinase in integrin-mediated signaling
    • Cary, L.A., and Guan, J.L. (1999) Focal adhesion kinase in integrin-mediated signaling. Front Biosci 4: D102-D113.
    • (1999) Front Biosci , vol.4
    • Cary, L.A.1    Guan, J.L.2
  • 8
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen, H.C., Appeddu, P.A., Isoda, H., and Guan, J.L. (1996) Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J Biol Chem 271: 26329-26334.
    • (1996) J Biol Chem , vol.271 , pp. 26329-26334
    • Chen, H.C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.L.4
  • 9
    • 70350181746 scopus 로고    scopus 로고
    • Identification of a Campylobacter jejuni-secreted protein required for maximal invasion of host cells
    • Christensen, J.E., Pacheco, S.A., and Konkel, M.E. (2009) Identification of a Campylobacter jejuni-secreted protein required for maximal invasion of host cells. Mol Microbiol 73: 650-662.
    • (2009) Mol Microbiol , vol.73 , pp. 650-662
    • Christensen, J.E.1    Pacheco, S.A.2    Konkel, M.E.3
  • 10
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: towards the systems level
    • Citri, A., and Yarden, Y. (2006) EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol 7: 505-516.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 11
    • 34548472221 scopus 로고    scopus 로고
    • GEF what? Dock180 and related proteins help Rac to polarize cells in new ways
    • Cote, J.F., and Vuori, K. (2007) GEF what? Dock180 and related proteins help Rac to polarize cells in new ways. Trends Cell Biol 17: 383-393.
    • (2007) Trends Cell Biol , vol.17 , pp. 383-393
    • Cote, J.F.1    Vuori, K.2
  • 12
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen, E.H., and Yamada, K.M. (2001) Fibronectin, integrins, and growth control. J Cell Physiol 189: 1-13.
    • (2001) J Cell Physiol , vol.189 , pp. 1-13
    • Danen, E.H.1    Yamada, K.M.2
  • 13
    • 38349137362 scopus 로고    scopus 로고
    • Epidermal growth factor stimulates Rac activation through Src and phosphatidylinositol 3-kinase to promote colonic epithelial cell migration
    • Dise, R.S., Frey, M.R., Whitehead, R.H., and Polk, D.B. (2008) Epidermal growth factor stimulates Rac activation through Src and phosphatidylinositol 3-kinase to promote colonic epithelial cell migration. Am J Physiol Gastrointest Liver Physiol 294: G276-G285.
    • (2008) Am J Physiol Gastrointest Liver Physiol , vol.294
    • Dise, R.S.1    Frey, M.R.2    Whitehead, R.H.3    Polk, D.B.4
  • 14
    • 0028918391 scopus 로고
    • Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK
    • Eide, B.L., Turck, C.W., and Escobedo, J.A. (1995) Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, pp125FAK. Mol Cell Biol 15: 2819-2827.
    • (1995) Mol Cell Biol , vol.15 , pp. 2819-2827
    • Eide, B.L.1    Turck, C.W.2    Escobedo, J.A.3
  • 15
    • 66549105468 scopus 로고    scopus 로고
    • Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization
    • Flanagan, R.C., Neal-McKinney, J.M., Dhillon, A.S., Miller, W.G., and Konkel, M.E. (2009) Examination of Campylobacter jejuni putative adhesins leads to the identification of a new protein, designated FlpA, required for chicken colonization. Infect Immun 77: 2399-2407.
    • (2009) Infect Immun , vol.77 , pp. 2399-2407
    • Flanagan, R.C.1    Neal-McKinney, J.M.2    Dhillon, A.S.3    Miller, W.G.4    Konkel, M.E.5
  • 16
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier, A., and Sonnenberg, A. (2001) Function and interactions of integrins. Cell Tissue Res 305: 285-298.
    • (2001) Cell Tissue Res , vol.305 , pp. 285-298
    • van der Flier, A.1    Sonnenberg, A.2
  • 17
    • 33845669072 scopus 로고    scopus 로고
    • Integrin signaling in epithelial cells
    • Gilcrease, M.Z. (2007) Integrin signaling in epithelial cells. Cancer Lett 247: 1-25.
    • (2007) Cancer Lett , vol.247 , pp. 1-25
    • Gilcrease, M.Z.1
  • 18
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279: 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 19
    • 0032765704 scopus 로고    scopus 로고
    • Campylobacter jejuni 81-176 associates with microtubules and dynein during invasion of human intestinal cells
    • Hu, L., and Kopecko, D.J. (1999) Campylobacter jejuni 81-176 associates with microtubules and dynein during invasion of human intestinal cells. Infect Immun 67: 4171-4182.
    • (1999) Infect Immun , vol.67 , pp. 4171-4182
    • Hu, L.1    Kopecko, D.J.2
  • 20
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O. (1992) Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 21
    • 0026625379 scopus 로고
    • Factors that influence the interaction of Campylobacter jejuni with cultured mammalian cells
    • Konkel, M.E., Corwin, M.D., Joens, L.A., and Cieplak, W. (1992) Factors that influence the interaction of Campylobacter jejuni with cultured mammalian cells. J Med Microbiol 37: 30-37.
    • (1992) J Med Microbiol , vol.37 , pp. 30-37
    • Konkel, M.E.1    Corwin, M.D.2    Joens, L.A.3    Cieplak, W.4
  • 22
    • 0030798150 scopus 로고    scopus 로고
    • Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni
    • Konkel, M.E., Garvis, S.G., Tipton, S.L., Anderson, D.E., Jr, and Cieplak, W., Jr (1997) Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol Microbiol 24: 953-963.
    • (1997) Mol Microbiol , vol.24 , pp. 953-963
    • Konkel, M.E.1    Garvis, S.G.2    Tipton, S.L.3    Anderson Jr., D.E.4    Cieplak Jr., W.5
  • 23
    • 0033016809 scopus 로고    scopus 로고
    • Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells
    • Konkel, M.E., Kim, B.J., Rivera-Amill, V., and Garvis, S.G. (1999) Bacterial secreted proteins are required for the internalization of Campylobacter jejuni into cultured mammalian cells. Mol Microbiol 32: 691-701.
    • (1999) Mol Microbiol , vol.32 , pp. 691-701
    • Konkel, M.E.1    Kim, B.J.2    Rivera-Amill, V.3    Garvis, S.G.4
  • 24
    • 2442705402 scopus 로고    scopus 로고
    • Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus
    • Konkel, M.E., Klena, J.D., Rivera-Amill, V., Monteville, M.R., Biswas, D., Raphael, B., and Mickelson, J. (2004) Secretion of virulence proteins from Campylobacter jejuni is dependent on a functional flagellar export apparatus. J Bacteriol 186: 3296-3303.
    • (2004) J Bacteriol , vol.186 , pp. 3296-3303
    • Konkel, M.E.1    Klena, J.D.2    Rivera-Amill, V.3    Monteville, M.R.4    Biswas, D.5    Raphael, B.6    Mickelson, J.7
  • 25
    • 73849129236 scopus 로고    scopus 로고
    • Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence
    • Konkel, M.E., Larson, C.L., and Flanagan, R.C. (2010) Campylobacter jejuni FlpA binds fibronectin and is required for maximal host cell adherence. J Bacteriol 192: 68-76.
    • (2010) J Bacteriol , vol.192 , pp. 68-76
    • Konkel, M.E.1    Larson, C.L.2    Flanagan, R.C.3
  • 26
    • 0035423127 scopus 로고    scopus 로고
    • Campylobacter jejuni - microtubule-dependent invasion
    • Kopecko, D.J., Hu, L., and Zaal, K.J. (2001) Campylobacter jejuni - microtubule-dependent invasion. Trends Microbiol 9: 389-396.
    • (2001) Trends Microbiol , vol.9 , pp. 389-396
    • Kopecko, D.J.1    Hu, L.2    Zaal, K.J.3
  • 27
    • 34548443431 scopus 로고    scopus 로고
    • Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni
    • Krause-Gruszczynska, M., Rohde, M., Hartig, R., Genth, H., Schmidt, G., Keo, T., etal. (2007) Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni. Cell Microbiol 9: 2431-2444.
    • (2007) Cell Microbiol , vol.9 , pp. 2431-2444
    • Krause-Gruszczynska, M.1    Rohde, M.2    Hartig, R.3    Genth, H.4    Schmidt, G.5    Keo, T.6
  • 28
    • 41549097842 scopus 로고    scopus 로고
    • Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression
    • Malik-Kale, P., Parker, C.T., and Konkel, M.E. (2008) Culture of Campylobacter jejuni with sodium deoxycholate induces virulence gene expression. J Bacteriol 190: 2286-2297.
    • (2008) J Bacteriol , vol.190 , pp. 2286-2297
    • Malik-Kale, P.1    Parker, C.T.2    Konkel, M.E.3
  • 29
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: in command and control of cell motility
    • Mitra, S.K., Hanson, D.A., and Schlaepfer, D.D. (2005) Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6: 56-68.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 30
    • 0031729477 scopus 로고    scopus 로고
    • Fibronectin and integrins in cell adhesion, signaling, and morphogenesis
    • Miyamoto, S., Katz, B.Z., Lafrenie, R.M., and Yamada, K.M. (1998) Fibronectin and integrins in cell adhesion, signaling, and morphogenesis. Ann N Y Acad Sci 857: 119-129.
    • (1998) Ann N Y Acad Sci , vol.857 , pp. 119-129
    • Miyamoto, S.1    Katz, B.Z.2    Lafrenie, R.M.3    Yamada, K.M.4
  • 31
    • 0037256265 scopus 로고    scopus 로고
    • Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization
    • Monteville, M.R., Yoon, J.E., and Konkel, M.E. (2003) Maximal adherence and invasion of INT 407 cells by Campylobacter jejuni requires the CadF outer-membrane protein and microfilament reorganization. Microbiology 149: 153-165.
    • (2003) Microbiology , vol.149 , pp. 153-165
    • Monteville, M.R.1    Yoon, J.E.2    Konkel, M.E.3
  • 32
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • Moro, L., Dolce, L., Cabodi, S., Bergatto, E., Boeri Erba, E., Smeriglio, M., etal. (2002) Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J Biol Chem 277: 9405-9414.
    • (2002) J Biol Chem , vol.277 , pp. 9405-9414
    • Moro, L.1    Dolce, L.2    Cabodi, S.3    Bergatto, E.4    Boeri Erba, E.5    Smeriglio, M.6
  • 33
    • 0027255262 scopus 로고
    • Unusual microtubule-dependent endocytosis mechanisms triggered by Campylobacter jejuni and Citrobacter freundii
    • Oelschlaeger, T.A., Guerry, P., and Kopecko, D.J. (1993) Unusual microtubule-dependent endocytosis mechanisms triggered by Campylobacter jejuni and Citrobacter freundii. Proc Natl Acad Sci USA 90: 6884-6888.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6884-6888
    • Oelschlaeger, T.A.1    Guerry, P.2    Kopecko, D.J.3
  • 34
    • 33750339742 scopus 로고    scopus 로고
    • Integrin traffic
    • Pellinen, T., and Ivaska, J. (2006) Integrin traffic. J Cell Sci 119: 3723-3731.
    • (2006) J Cell Sci , vol.119 , pp. 3723-3731
    • Pellinen, T.1    Ivaska, J.2
  • 35
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M., and Hall, A. (2004) Cell migration: Rho GTPases lead the way. Dev Biol 265: 23-32.
    • (2004) Dev Biol , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 36
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., Paterson, H.F., Johnston, C.L., Diekmann, D., and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 37
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K.G., Ying, Y.S., Kamen, B.A., and Anderson, R.G. (1990) Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J Cell Biol 111: 2931-2938.
    • (1990) J Cell Biol , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.4
  • 38
    • 33847082547 scopus 로고    scopus 로고
    • The health burden of Campylobacter infection and the impact of antimicrobial resistance: playing chicken
    • Ruiz-Palacios, G.M. (2007) The health burden of Campylobacter infection and the impact of antimicrobial resistance: playing chicken. Clin Infect Dis 44: 701-703.
    • (2007) Clin Infect Dis , vol.44 , pp. 701-703
    • Ruiz-Palacios, G.M.1
  • 39
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller, M.D., Otey, C.A., Hildebrand, J.D., and Parsons, J.T. (1995) Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J Cell Biol 130: 1181-1187.
    • (1995) J Cell Biol , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 41
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer, J.E., Oh, P., Pinney, E., and Allard, J. (1994) Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J Cell Biol 127: 1217-1232.
    • (1994) J Cell Biol , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 42
    • 12844269776 scopus 로고    scopus 로고
    • Fibronectin matrix turnover occurs through a caveolin-1-dependent process
    • Sottile, J., and Chandler, J. (2005) Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Mol Biol Cell 16: 757-768.
    • (2005) Mol Biol Cell , vol.16 , pp. 757-768
    • Sottile, J.1    Chandler, J.2
  • 43
    • 0028980418 scopus 로고
    • Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK
    • Tachibana, K., Sato, T., D'Avirro, N., and Morimoto, C. (1995) Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J Exp Med 182: 1089-1099.
    • (1995) J Exp Med , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 44
    • 17844406391 scopus 로고    scopus 로고
    • Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells
    • Thelemann, A., Petti, F., Griffin, G., Iwata, K., Hunt, T., Settinari, T., etal. (2005) Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol Cell Proteomics 4: 356-376.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 356-376
    • Thelemann, A.1    Petti, F.2    Griffin, G.3    Iwata, K.4    Hunt, T.5    Settinari, T.6
  • 45
    • 0031694935 scopus 로고    scopus 로고
    • Integrin signaling: tyrosine phosphorylation events in focal adhesions
    • Vuori, K. (1998) Integrin signaling: tyrosine phosphorylation events in focal adhesions. J Membr Biol 165: 191-199.
    • (1998) J Membr Biol , vol.165 , pp. 191-199
    • Vuori, K.1
  • 46
    • 0030273597 scopus 로고    scopus 로고
    • Host signal transduction and endocytosis of Campylobacter jejuni
    • Wooldridge, K.G., Williams, P.H., and Ketley, J.M. (1996) Host signal transduction and endocytosis of Campylobacter jejuni. Microb Pathog 21: 299-305.
    • (1996) Microb Pathog , vol.21 , pp. 299-305
    • Wooldridge, K.G.1    Williams, P.H.2    Ketley, J.M.3
  • 47
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E., and Geiger, B. (2001) Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci 114: 3583-3590.
    • (2001) J Cell Sci , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2


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