메뉴 건너뛰기




Volumn 117, Issue 17, 2004, Pages 3923-3933

Analysis of Chlamydia caviae entry sites and involvement of Cdc42 and Rac activity

Author keywords

Actin polymerization; Chlamydiaceae; Lipid rafts; Phagocytosis; PI 3 kinase; Small GTPases

Indexed keywords

GANGLIOSIDE GM1; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN CDC42; RAC PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 4444254395     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01247     Document Type: Article
Times cited : (62)

References (50)
  • 2
    • 0028131926 scopus 로고
    • Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation during uptake by HeLa cells
    • Birkelund, S., Johnsen, H. and Christiansen, G. (1994). Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation during uptake by HeLa cells. Infect. Immun. 62, 4900-4908.
    • (1994) Infect. Immun. , vol.62 , pp. 4900-4908
    • Birkelund, S.1    Johnsen, H.2    Christiansen, G.3
  • 3
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A. L. and Hall, A. (2000). Rho GTPases and their effector proteins. Biochem. J. 348, 241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 4
    • 0032977966 scopus 로고    scopus 로고
    • Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: Clathrin-independent entry into cells and dynamin-dependent productive growth
    • Boleti, H., Benmerah, A., Ojcius, D., Cerf-Bensussan, N. and Dautry-Varsat, A. (1999). Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: clathrin-independent entry into cells and dynamin-dependent productive growth. J. Cell Sci. 112, 1487-1496.
    • (1999) J. Cell Sci. , vol.112 , pp. 1487-1496
    • Boleti, H.1    Benmerah, A.2    Ojcius, D.3    Cerf-Bensussan, N.4    Dautry-Varsat, A.5
  • 5
    • 0038062664 scopus 로고    scopus 로고
    • Bacterial virulence factors targeting Rho GTPases: Parasitism or symbiosis?
    • Boquet, P. and Lemichez, E. (2003). Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis? Trend. Cell Biol. 13, 238-246.
    • (2003) Trend Cell Biol. , vol.13 , pp. 238-246
    • Boquet, P.1    Lemichez, E.2
  • 6
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., Drechsel, D. and Hall, A. (1995). A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270, 29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 7
    • 0017843491 scopus 로고
    • Kinetics of phagocytosis of Chlamydia-psittaci by mouse fibroblasts (L-Cells) - Separation of attachment and ingestion stages
    • Byrne, G. I. (1978). Kinetics of phagocytosis of Chlamydia-psittaci by mouse fibroblasts (L-Cells) - separation of attachment and ingestion stages. Infect. Immun. 19, 607-612.
    • (1978) Infect. Immun. , vol.19 , pp. 607-612
    • Byrne, G.I.1
  • 8
    • 0036081413 scopus 로고    scopus 로고
    • Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells
    • Carabeo, R. A., Grieshaber, S. S., Fischer, E. and Hackstadt, T. (2002). Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells. Infect. Immun. 70, 3793-3803.
    • (2002) Infect. Immun. , vol.70 , pp. 3793-3803
    • Carabeo, R.A.1    Grieshaber, S.S.2    Fischer, E.3    Hackstadt, T.4
  • 9
    • 0032573378 scopus 로고    scopus 로고
    • Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases
    • Caron, E. and Hall, A. (1998). Identification of two distinct mechanisms of phagocytosis controlled by different Rho GTPases. Science 282, 1717-1721.
    • (1998) Science , vol.282 , pp. 1717-1721
    • Caron, E.1    Hall, A.2
  • 10
    • 0036326980 scopus 로고    scopus 로고
    • Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells
    • Coombes, B. K. and Mahony, J. B. (2002). Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells. Cell. Microbiol. 4, 447-460.
    • (2002) Cell. Microbiol. , vol.4 , pp. 447-460
    • Coombes, B.K.1    Mahony, J.B.2
  • 11
    • 0033555931 scopus 로고    scopus 로고
    • A requirement for phosphatidylinositol 3-kinase in pseudopod extension
    • Cox, D., Tseng, C. C., Bjekic, G. and Greenberg, S. (1999). A requirement for phosphatidylinositol 3-kinase in pseudopod extension. J. Biol. Chem. 274, 1240-1247.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1240-1247
    • Cox, D.1    Tseng, C.C.2    Bjekic, G.3    Greenberg, S.4
  • 12
    • 0035040115 scopus 로고    scopus 로고
    • The GTPase Rac1 selectively regulates Salmonella invasion at the apical plasma membrane of polarized epithelial cells
    • Criss, A. K., Ahlgren, D. M., Jou, T. S., McCormick, B. A. and Casanova, J. E. (2001). The GTPase Rac1 selectively regulates Salmonella invasion at the apical plasma membrane of polarized epithelial cells. J. Cell Sci. 114, 1331-1341.
    • (2001) J. Cell Sci. , vol.114 , pp. 1331-1341
    • Criss, A.K.1    Ahlgren, D.M.2    Jou, T.S.3    McCormick, B.A.4    Casanova, J.E.5
  • 13
    • 0016799225 scopus 로고
    • Comparative susceptibility of 11 mammalian-cell lines to infection with trachoma organisms
    • Croy, T. R., Kuo, C. C. and Wang, S. P. (1975). Comparative susceptibility of 11 mammalian-cell lines to infection with trachoma organisms. J. Clin. Microbiol. 1, 434-439.
    • (1975) J. Clin. Microbiol. , vol.1 , pp. 434-439
    • Croy, T.R.1    Kuo, C.C.2    Wang, S.P.3
  • 14
    • 0030782168 scopus 로고    scopus 로고
    • Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin
    • Fawaz, F. S., van Ooij, C., Homola, E., Mutka, S. C. and Engel, J. N. (1997). Infection with Chlamydia trachomatis alters the tyrosine phosphorylation and/or localization of several host cell proteins including cortactin. Infect. Immun. 65, 5301-5308.
    • (1997) Infect. Immun. , vol.65 , pp. 5301-5308
    • Fawaz, F.S.1    van Ooij, C.2    Homola, E.3    Mutka, S.C.4    Engel, J.N.5
  • 15
    • 0038011417 scopus 로고    scopus 로고
    • Chlamydia trachomatis type III secretion: Evidence for a functional apparatus during early-cycle development
    • Fields, K. A., Mead, D. J., Dooley, C. A. and Hackstadt, T. (2003). Chlamydia trachomatis type III secretion: evidence for a functional apparatus during early-cycle development. Mol. Microbiol. 48, 671-683.
    • (2003) Mol. Microbiol. , vol.48 , pp. 671-683
    • Fields, K.A.1    Mead, D.J.2    Dooley, C.A.3    Hackstadt, T.4
  • 16
    • 0015336859 scopus 로고
    • Interaction of L cells and Chlamydia psittaci: Entry of the parasite and host responses to its development
    • Friis, R. R. (1972). Interaction of L cells and Chlamydia psittaci: entry of the parasite and host responses to its development. J. Bacteriol. 110, 706-721.
    • (1972) J. Bacteriol. , vol.110 , pp. 706-721
    • Friis, R.R.1
  • 19
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., Calalb, M. B., Harper, M. C. and Patel, S. K. (1992). Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89, 8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 20
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder, T. and Simons, K. (1999). Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur. J. Immunol. 29, 556-562.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 21
    • 0032577563 scopus 로고    scopus 로고
    • S-typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt, W. D., Chen, L. M., Schuebel, K. E., Bustelo, X. R. and Galan, J. E. (1998). S-typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93, 815-826.
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galan, J.E.5
  • 22
    • 0023906752 scopus 로고
    • Ultrastructural study of endocytosis of Chlamydia trachomatis by McCoy cells
    • Hodinka, R. L., Davis, C. H., Choong, J. and Wyrick, P. B. (1988). Ultrastructural study of endocytosis of Chlamydia trachomatis by McCoy cells. Infect. Immun. 56, 1456-1463.
    • (1988) Infect. Immun. , vol.56 , pp. 1456-1463
    • Hodinka, R.L.1    Davis, C.H.2    Choong, J.3    Wyrick, P.B.4
  • 23
    • 0037220583 scopus 로고    scopus 로고
    • Entry of the lymphogranuloma venereum strain of Chlamydia trachomatis into host cells involves cholesterol-rich membrane domains
    • Jutras, I., Abrami, L. and Dautry-Varsat, A. (2003). Entry of the lymphogranuloma venereum strain of Chlamydia trachomatis into host cells involves cholesterol-rich membrane domains. Infect. Immun. 71, 260-266.
    • (2003) Infect. Immun. , vol.71 , pp. 260-266
    • Jutras, I.1    Abrami, L.2    Dautry-Varsat, A.3
  • 25
    • 0023929267 scopus 로고
    • Ultrastructural study for entry of Chlamydia strain TWAR into HeLa cells
    • Kuo, C. C., Chi, E. and Grayston, J. (1988). Ultrastructural study for entry of Chlamydia strain TWAR into HeLa cells. Infect. Immun. 56, 1668-1672.
    • (1988) Infect. Immun. , vol.56 , pp. 1668-1672
    • Kuo, C.C.1    Chi, E.2    Grayston, J.3
  • 27
    • 0012108774 scopus 로고
    • Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells
    • Maher, P. A., Pasquale, E. B., Wang, J. Y. J. and Singer, S. J. (1985). Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc. Natl. Acad. Sci. USA 82, 6576-6580.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6576-6580
    • Maher, P.A.1    Pasquale, E.B.2    Wang, J.Y.J.3    Singer, S.J.4
  • 28
    • 0028078824 scopus 로고
    • A brain serine threonine protein-kinase activated by Cdc42 and Rac1
    • Manser, E., Leung, T., Salihuddin, H., Zhao, Z. S. and Lim, L. (1994). A brain serine threonine protein-kinase activated by Cdc42 and Rac1. Nature 367, 40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 29
    • 0036158774 scopus 로고    scopus 로고
    • Requirement of Rho-family GTPases in the invasion of type 1-piliated uropathogenic Escherichia coli
    • Martinez, J. J. and Hultgren, S. J. (2002). Requirement of Rho-family GTPases in the invasion of type 1-piliated uropathogenic Escherichia coli. Cell. Microbiol. 4, 19-28.
    • (2002) Cell. Microbiol. , vol.4 , pp. 19-28
    • Martinez, J.J.1    Hultgren, S.J.2
  • 30
    • 0032476593 scopus 로고    scopus 로고
    • Fc receptor-mediated phagocytosis requires CPC42 and Rac1
    • Massol, P., Montcourrier, P., Guillemot, J. C. and Chavrier, P. (1998). Fc receptor-mediated phagocytosis requires CPC42 and Rac1. EMBO J. 17, 6219-6229.
    • (1998) EMBO J. , vol.17 , pp. 6219-6229
    • Massol, P.1    Montcourrier, P.2    Guillemot, J.C.3    Chavrier, P.4
  • 31
    • 0031799850 scopus 로고    scopus 로고
    • The Yersinia Yops inhibit invasion of Listeria, Shigella and Edwardsiella but not Salmonella into epithelial cells
    • Mecsas, J., Raupach, B. and Falkow, S. (1998). The Yersinia Yops inhibit invasion of Listeria, Shigella and Edwardsiella but not Salmonella into epithelial cells. Mol. Microbiol. 28, 1269-1281.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1269-1281
    • Mecsas, J.1    Raupach, B.2    Falkow, S.3
  • 32
    • 0032839369 scopus 로고    scopus 로고
    • Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility
    • Mounier, J., Laurent, V., Hall, A., Fort, P., Cartier, M. F., Sansonetti, P. J. and Egile, C. (1999). Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. J. Cell Sci. 112, 2069-2080.
    • (1999) J. Cell Sci. , vol.112 , pp. 2069-2080
    • Mounier, J.1    Laurent, V.2    Hall, A.3    Fort, P.4    Cartier, M.F.5    Sansonetti, P.J.6    Egile, C.7
  • 33
    • 0032546654 scopus 로고    scopus 로고
    • Activation of G(1) progression, JNK mitogen-activated protein kinase, and actin filament assembly by the exchange factor FGD1
    • Nagata, K., Driessens, M., Lamarche, N., Gorski, J. L. and Hall, A. (1998). Activation of G(1) progression, JNK mitogen-activated protein kinase, and actin filament assembly by the exchange factor FGD1. J. Biol. Chem. 273, 15453-15457.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15453-15457
    • Nagata, K.1    Driessens, M.2    Lamarche, N.3    Gorski, J.L.4    Hall, A.5
  • 34
    • 0034949325 scopus 로고    scopus 로고
    • Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection
    • Norkin, L. C., Wolfrom, S. A. and Stuart, E. S. (2001). Association of caveolin with Chlamydia trachomatis inclusions at early and late stages of infection. Exp. Cell Res. 266, 229-238.
    • (2001) Exp. Cell Res. , vol.266 , pp. 229-238
    • Norkin, L.C.1    Wolfrom, S.A.2    Stuart, E.S.3
  • 35
    • 0027525563 scopus 로고
    • Molecular characterization and outer membrane association of a Chlamydia trachomatis protein related to the hsp70 family of proteins
    • Raulston, J. E., Davis, C. H., Schmiel, D. H., Morgan, M. W. and Wyrick, P. B. (1993). Molecular characterization and outer membrane association of a Chlamydia trachomatis protein related to the hsp70 family of proteins. J. Biol. Chem. 268, 23139-23147.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23139-23147
    • Raulston, J.E.1    Davis, C.H.2    Schmiel, D.H.3    Morgan, M.W.4    Wyrick, P.B.5
  • 36
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • Shin, J. S., Gao, Z. M. and Abraham, S. N. (2000). Involvement of cellular caveolae in bacterial entry into mast cells. Science 289, 785-788.
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.S.1    Gao, Z.M.2    Abraham, S.N.3
  • 37
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons, K. and Ehehalt, R. (2002). Cholesterol, lipid rafts, and disease. J. Clin. Invest. 110, 597-603.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 39
    • 0033381544 scopus 로고    scopus 로고
    • Chlamydia trachomatis infections: Progress and problems
    • Stamm, W. E. (1999). Chlamydia trachomatis infections: progress and problems. J. Infect. Dis. 179, S380-S383.
    • (1999) J. Infect. Dis. , vol.179
    • Stamm, W.E.1
  • 40
    • 0019833573 scopus 로고
    • The cholera toxin receptor ganglioside GM remains associated with Triton X-100 cytoskeletons of BALB/c-3T3 cells
    • Streuli, C. H., Patel, B. and Critchley, D. R. (1981). The cholera toxin receptor ganglioside GM remains associated with Triton X-100 cytoskeletons of BALB/c-3T3 cells. Exp. Cell Res. 136, 247-254.
    • (1981) Exp. Cell Res. , vol.136 , pp. 247-254
    • Streuli, C.H.1    Patel, B.2    Critchley, D.R.3
  • 41
    • 0037530035 scopus 로고    scopus 로고
    • Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells
    • Stuart, E. S., Webiey, W. C. and Norkin, L. C. (2003). Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells. Exp. Cell Res. 287, 67-78.
    • (2003) Exp. Cell Res. , vol.287 , pp. 67-78
    • Stuart, E.S.1    Webiey, W.C.2    Norkin, L.C.3
  • 42
    • 0029743307 scopus 로고    scopus 로고
    • A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells
    • Su, H., Raymond, L., Rockey, D. D., Fischer, E., Hackstadt, T. and Caldwell, H. D. (1996). A recombinant Chlamydia trachomatis major outer membrane protein binds to heparan sulfate receptors on epithelial cells. Proc. Nutl. Acad. Sci. USA 93, 11143-11148.
    • (1996) Proc. Nutl. Acad. Sci. USA , vol.93 , pp. 11143-11148
    • Su, H.1    Raymond, L.2    Rockey, D.D.3    Fischer, E.4    Hackstadt, T.5    Caldwell, H.D.6
  • 43
    • 0029123843 scopus 로고
    • Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface
    • Ting, L. M., Hsia, R. C., Haidaris, C. G. and Bavoil, P. M. (1995). Interaction of outer envelope proteins of Chlamydia psittaci GPIC with the HeLa cell surface. Infect. Immun. 63, 3600-3608.
    • (1995) Infect. Immun. , vol.63 , pp. 3600-3608
    • Ting, L.M.1    Hsia, R.C.2    Haidaris, C.G.3    Bavoil, P.M.4
  • 44
    • 0037474290 scopus 로고    scopus 로고
    • Differential role of actin, clathrin, and dynamin in Fcγ receptor-mediated endocytosis and phagocytosis
    • Tse, S. M. L., Furuya, W., Gold, E., Schreiber, A. D., Sandvig, K., Inman, R. D. and Grinstein, S. (2003). Differential role of actin, clathrin, and dynamin in Fcγ receptor-mediated endocytosis and phagocytosis. J. Biol. Chem. 278, 3331-3338.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3331-3338
    • Tse, S.M.L.1    Furuya, W.2    Gold, E.3    Schreiber, A.D.4    Sandvig, K.5    Inman, R.D.6    Grinstein, S.7
  • 45
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: Complexity in action
    • Underhill, D. M. and Ozinsky, A. (2002). Phagocytosis of microbes: complexity in action. Annu. Rev. Immunol. 20, 825-852.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 46
    • 0345593392 scopus 로고    scopus 로고
    • IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells
    • Van Nhieu, G. T., Caron, E., Hall, A. and Sansonetti, P. J. (1999). IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells. EMBO J. 18, 3249-3262.
    • (1999) EMBO J. , vol.18 , pp. 3249-3262
    • Van Nhieu, G.T.1    Caron, E.2    Hall, A.3    Sansonetti, P.J.4
  • 48
    • 0021134763 scopus 로고
    • Control mechanisms governing the infectivity of Chlamydia trachomatis for HeLa cells: Mechanisms of endocytosis
    • Ward, M. E. and Murray, A. (1984). Control mechanisms governing the infectivity of Chlamydia trachomatis for HeLa cells: mechanisms of endocytosis. J. Gen. Microbiol. 130, 1765-1780.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 1765-1780
    • Ward, M.E.1    Murray, A.2
  • 50
    • 0026622894 scopus 로고
    • Mechanism of Chlamydia trachomatis attachment to eukaryotic host cells
    • Zhang, J. P. and Stephens, R. S. (1992). Mechanism of Chlamydia trachomatis attachment to eukaryotic host cells. Cell 69, 861-869.
    • (1992) Cell , vol.69 , pp. 861-869
    • Zhang, J.P.1    Stephens, R.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.