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Volumn 990, Issue , 2003, Pages 535-547

Rickettsial actin-based motility: Behavior and involvement of cytoskeletal regulators

Author keywords

Actin; Arp2 3 complex; Motility; N WASP; Rickettsia

Indexed keywords

ACTIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 0037713720     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb07424.x     Document Type: Conference Paper
Times cited : (59)

References (38)
  • 1
    • 0035199154 scopus 로고    scopus 로고
    • Actin-based motility of intracellular microbial pathogens
    • GOLDBERG, M.B. 2001. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65: 595-626.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 595-626
    • Goldberg, M.B.1
  • 2
    • 0027086804 scopus 로고
    • Intracellular movements of Rickettsia conorii and R. typhi based on actin polymerization
    • TEYSSIERE, N., C. CHICHE-PORTICHE & D. RAOULT. 1992. Intracellular movements of Rickettsia conorii and R. typhi based on actin polymerization. Res. Microbiol. 143: 821-829.
    • (1992) Res. Microbiol. , vol.143 , pp. 821-829
    • Teyssiere, N.1    Chiche-Portiche, C.2    Raoult, D.3
  • 3
    • 0027230730 scopus 로고
    • Directional actin polymerization associated with spotted fever group rickettsia infection of Vero cells
    • HEINZEN, R.A., S.F. HAYES, M.G. PEACOCK & T. HACKSTADT. 1993. Directional actin polymerization associated with spotted fever group rickettsia infection of Vero cells. Infect. Immun. 61: 1926-1935.
    • (1993) Infect. Immun. , vol.61 , pp. 1926-1935
    • Heinzen, R.A.1    Hayes, S.F.2    Peacock, M.G.3    Hackstadt, T.4
  • 4
    • 0032768668 scopus 로고    scopus 로고
    • Dynamics of actin-based movement by Rickettsia rickettsii in Vero cells
    • HEINZEN, R.A., S.S. GRIESHABER, L.S. VAN KIRK & C.J. DEVIN. 1999. Dynamics of actin-based movement by Rickettsia rickettsii in Vero cells. Infect. Immun. 67: 4201-4207.
    • (1999) Infect. Immun. , vol.67 , pp. 4201-4207
    • Heinzen, R.A.1    Grieshaber, S.S.2    Van Kirk, L.S.3    Devin, C.J.4
  • 5
    • 0033055077 scopus 로고    scopus 로고
    • A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri, and Rickettsia conorii
    • GOUIN, E. et al. 1999. A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri, and Rickettsia conorii. J. Cell Sci. 112: 1697-1708.
    • (1999) J. Cell Sci. , vol.112 , pp. 1697-1708
    • Gouin, E.1
  • 6
    • 0033914895 scopus 로고    scopus 로고
    • Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins
    • VAN KIRK, L.S., S.F. HAYES & R.A. HEINZEN. 2000. Ultrastructure of Rickettsia rickettsii actin tails and localization of cytoskeletal proteins. Infect. Immun. 68: 4706-4713.
    • (2000) Infect. Immun. , vol.68 , pp. 4706-4713
    • Van Kirk, L.S.1    Hayes, S.F.2    Heinzen, R.A.3
  • 7
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • EGILE, C. et al. 1999. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146: 1319-1332.
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1332
    • Egile, C.1
  • 8
    • 0036468733 scopus 로고    scopus 로고
    • Regulation of Wiskott-Aldrich syndrome protein and related molecules
    • CARON, E. 2002. Regulation of Wiskott-Aldrich syndrome protein and related molecules. Curr. Opin. Cell Biol. 14: 82-87.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 82-87
    • Caron, E.1
  • 9
    • 0032525132 scopus 로고    scopus 로고
    • Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri
    • SUZUKI, T., H. MIKI, T. TAKENAWA & C. SASAKAWA. 1998. Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17: 2767-2776.
    • (1998) EMBO J. , vol.17 , pp. 2767-2776
    • Suzuki, T.1    Miki, H.2    Takenawa, T.3    Sasakawa, C.4
  • 10
    • 0033960791 scopus 로고    scopus 로고
    • How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures
    • MULLINS, R.D. 2000. How WASP-family proteins and the Arp2/3 complex convert intracellular signals into cytoskeletal structures. Curr. Opin. Cell Biol. 12: 91-96.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 91-96
    • Mullins, R.D.1
  • 11
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5- bisphosphate
    • ROHATGI, R., H.Y. HO & M.W. KIRSCHNER. 2000. Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5- bisphosphate. J. Cell Biol. 150: 1299-1310.
    • (2000) J. Cell Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 12
    • 0033616763 scopus 로고    scopus 로고
    • Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
    • MACHESKY, L.M. et al. 1999. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl. Acad. Sci. USA 96: 3739-3744.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3739-3744
    • Machesky, L.M.1
  • 13
    • 0033040628 scopus 로고    scopus 로고
    • The Arp2/3 complex: A multifunctional actin organizer
    • MACHESKY, L.M. & K.L. GOULD. 1999. The Arp2/3 complex: a multifunctional actin organizer. Curr. Opin. Cell Biol. 11: 117-121.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 117-121
    • Machesky, L.M.1    Gould, K.L.2
  • 14
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • WELCH, M.D., A. IWAMATSU & T.J. MITCHISON. 1997. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385: 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 15
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • WELCH, M.D. et al. 1998. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281: 105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1
  • 16
    • 0035949529 scopus 로고    scopus 로고
    • Listeria protein ActA mimics WASp family proteins: It activates filament barbed end branching by Arp2/3 complex
    • BOUJEMAA-PATERSKI, R. et al. 2001. Listeria protein ActA mimics WASp family proteins: it activates filament barbed end branching by Arp2/3 complex. Biochemistry 40: 11390-11404.
    • (2001) Biochemistry , vol.40 , pp. 11390-11404
    • Boujemaa-Paterski, R.1
  • 17
    • 0033780474 scopus 로고    scopus 로고
    • A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization
    • MOREAU, V. et al. 2000. A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell. Biol. 2: 441-448.
    • (2000) Nat. Cell. Biol. , vol.2 , pp. 441-448
    • Moreau, V.1
  • 18
    • 0016777988 scopus 로고
    • Separation of viable Rickettsia typhi from yolk sac and L cell host components by renografin density gradient centrifugation
    • WEISS, E., J.C. COOLBAUGH & J.C. WILLIAMS. 1975. Separation of viable Rickettsia typhi from yolk sac and L cell host components by renografin density gradient centrifugation. Appl. Microbiol. 30: 456-463.
    • (1975) Appl. Microbiol. , vol.30 , pp. 456-463
    • Weiss, E.1    Coolbaugh, J.C.2    Williams, J.C.3
  • 19
    • 0034861061 scopus 로고    scopus 로고
    • Cryptosporidium parvum infection requires host cell actin polymerization
    • ELLIOTT, D.A. et al. 2001. Cryptosporidium parvum infection requires host cell actin polymerization. Infect. Immun. 69: 5940-5942.
    • (2001) Infect. Immun. , vol.69 , pp. 5940-5942
    • Elliott, D.A.1
  • 20
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • LOMMEL, S. et al. 2001. Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2: 850-857.
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1
  • 21
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • TAPON, N. & A. HALL. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9: 86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 22
    • 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. & R.H. INSALL. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8: 1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 23
    • 0033790639 scopus 로고    scopus 로고
    • Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3
    • MAY, R.C., E. CARON, A. HALL & L.M. MACHESKY. 2000. Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3. Nat. Cell Biol. 2: 246-248.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 246-248
    • May, R.C.1    Caron, E.2    Hall, A.3    Machesky, L.M.4
  • 24
    • 0033853186 scopus 로고    scopus 로고
    • Actin-based motility of pathogens: The Arp2/3 complex is a central player
    • COSSART, P. 2000. Actin-based motility of pathogens: the Arp2/3 complex is a central player. Cell. Microbiol. 2: 195-205.
    • (2000) Cell. Microbiol. , vol.2 , pp. 195-205
    • Cossart, P.1
  • 25
    • 0035159257 scopus 로고    scopus 로고
    • Efficient uptake of Yersinia pseudotuberculosis via integrin receptors involves a Rac1-Arp 2/3 pathway that bypasses N-WASP function
    • ALRUTZ, M.A. et al. 2001. Efficient uptake of Yersinia pseudotuberculosis via integrin receptors involves a Rac1-Arp 2/3 pathway that bypasses N-WASP function. Mol. Microbiol. 42: 689-703.
    • (2001) Mol. Microbiol. , vol.42 , pp. 689-703
    • Alrutz, M.A.1
  • 26
    • 0035976859 scopus 로고    scopus 로고
    • A role for N-WASP in invasin-promoted internalisation
    • MCGEE, K., M. ZETTL, M. WAY & M. FALLMAN. 2001. A role for N-WASP in invasin-promoted internalisation. FEBS Lett. 509: 59-65.
    • (2001) FEBS Lett. , vol.509 , pp. 59-65
    • Mcgee, K.1    Zettl, M.2    Way, M.3    Fallman, M.4
  • 27
    • 0033740788 scopus 로고    scopus 로고
    • Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP
    • YAMAGUCHI, H. et al. 2000. Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation by N-WASP. Proc. Natl. Acad. Sci. USA 97: 12631-12636.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12631-12636
    • Yamaguchi, H.1
  • 28
    • 0033565599 scopus 로고    scopus 로고
    • The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes
    • MAY, R.C. et al. 1999. The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes. Curr. Biol. 9: 759-762.
    • (1999) Curr. Biol. , vol.9 , pp. 759-762
    • May, R.C.1
  • 29
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • PRUYNE, D. et al. 2002. Role of formins in actin assembly: nucleation and barbed-end association. Science 297: 612-615.
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1
  • 30
    • 0034906978 scopus 로고    scopus 로고
    • ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity
    • FRADELIZI, J. et al. 2001. ActA and human zyxin harbour Arp2/3-independent actin-polymerization activity. Nat. Cell Biol. 3: 699-707.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 699-707
    • Fradelizi, J.1
  • 31
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • THERIOT, J.A., T.J. MITCHISON, L.G. TILNEY & D.A. PORTNOY. 1992. The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357: 257-260.
    • (1992) Nature , vol.357 , pp. 257-260
    • Theriot, J.A.1    Mitchison, T.J.2    Tilney, L.G.3    Portnoy, D.A.4
  • 32
    • 0016075695 scopus 로고
    • Plaque assay of rickettsiae in a mammalian cell line
    • CORY, J. et al. 1974. Plaque assay of rickettsiae in a mammalian cell line. Appl. Microbiol. 27: 1157-1161.
    • (1974) Appl. Microbiol. , vol.27 , pp. 1157-1161
    • Cory, J.1
  • 34
    • 0024362336 scopus 로고
    • Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin
    • BERNARDINI, M.L. et al. 1989. Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin. Proc. Natl. Acad. Sci. USA 86: 3867-3871.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3867-3871
    • Bernardini, M.L.1
  • 35
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • KOCKS, C. et al. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68: 521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1
  • 36
    • 0034843552 scopus 로고    scopus 로고
    • Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake
    • MONACK, D.M. & J.A. THERIOT. 2001. Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake. Cell. Microbiol. 3, 633-647.
    • (2001) Cell. Microbiol. , vol.3 , pp. 633-647
    • Monack, D.M.1    Theriot, J.A.2
  • 37
    • 0025153771 scopus 로고
    • Rickettsia species (as organisms)
    • WINKLER, H.H. 1990. Rickettsia species (as organisms). Annu. Rev. Microbiol. 44: 131-153.
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 131-153
    • Winkler, H.H.1


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