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Volumn 420, Issue 4, 2012, Pages 816-821

Chlamydia trachomatis Tarp cooperates with the Arp2/3 complex to increase the rate of actin polymerization

Author keywords

Actin; Arp2 3 complex; Chlamydia trachomatis; Tarp

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; BACTERIAL PROTEIN; PHOSPHOPROTEIN; TRANSLOCATED ACTIN RECRUITING PHOSPHOPROTEIN; UNCLASSIFIED DRUG;

EID: 84859849027     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.03.080     Document Type: Article
Times cited : (38)

References (31)
  • 1
    • 79954468455 scopus 로고    scopus 로고
    • CDC Grand Rounds: Chlamydia prevention: challenges and strategies for reducing disease burden and sequelae
    • MMWR Morb Mortal Wkly Rep
    • CDC Grand Rounds: Chlamydia prevention: challenges and strategies for reducing disease burden and sequelae. MMWR Morb Mortal Wkly Rep 60 370-373.
    • , vol.60 , pp. 370-373
  • 4
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske K., Stephens R.S. Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc. Natl. Acad. Sci. USA 2007, 104:11430-11435.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.S.2
  • 5
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder J.W. Interaction of chlamydiae and host cells in vitro. Microbiol. Rev. 1991, 55:143-190.
    • (1991) Microbiol. Rev. , vol.55 , pp. 143-190
    • Moulder, J.W.1
  • 6
    • 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., Hackstadt T. Chlamydia trachomatis induces remodeling of the actin cytoskeleton during attachment and entry into HeLa cells. Infect. Immun. 2002, 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
  • 7
    • 34547871262 scopus 로고    scopus 로고
    • Rac interacts with Abi-1 and WAVE2 to promote an Arp2/3-dependent actin recruitment during chlamydial invasion
    • Carabeo R.A., Dooley C.A., Grieshaber S.S., Hackstadt T. Rac interacts with Abi-1 and WAVE2 to promote an Arp2/3-dependent actin recruitment during chlamydial invasion. Cell Microbiol. 2007, 9:2278-2288.
    • (2007) Cell Microbiol. , vol.9 , pp. 2278-2288
    • Carabeo, R.A.1    Dooley, C.A.2    Grieshaber, S.S.3    Hackstadt, T.4
  • 8
    • 34547621080 scopus 로고    scopus 로고
    • Mechanisms of Chlamydia trachomatis entry into nonphagocytic cells
    • Hybiske K., Stephens R.S. Mechanisms of Chlamydia trachomatis entry into nonphagocytic cells. Infect. Immun. 2007, 75:3925-3934.
    • (2007) Infect. Immun. , vol.75 , pp. 3925-3934
    • Hybiske, K.1    Stephens, R.S.2
  • 11
    • 77957686132 scopus 로고    scopus 로고
    • The conserved Tarp actin binding domain is important for chlamydial invasion
    • Jewett T.J., Miller N.J., Dooley C.A., Hackstadt T. The conserved Tarp actin binding domain is important for chlamydial invasion. PLoS Pathog. 2010, 6:e1000997.
    • (2010) PLoS Pathog. , vol.6
    • Jewett, T.J.1    Miller, N.J.2    Dooley, C.A.3    Hackstadt, T.4
  • 12
    • 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 R.D., 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 1998, 95:6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 13
    • 0031051993 scopus 로고    scopus 로고
    • Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba
    • Mullins R.D., Stafford W.F., Pollard T.D. Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba. J. Cell. Biol. 1997, 136:331-343.
    • (1997) J. Cell. Biol. , vol.136 , pp. 331-343
    • Mullins, R.D.1    Stafford, W.F.2    Pollard, T.D.3
  • 14
    • 0030802671 scopus 로고    scopus 로고
    • The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly
    • Welch M.D., DePace A.H., Verma S., Iwamatsu A., Mitchison T.J. The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. J. Cell. Biol. 1997, 138:375-384.
    • (1997) J. Cell. Biol. , vol.138 , pp. 375-384
    • Welch, M.D.1    DePace, A.H.2    Verma, S.3    Iwamatsu, A.4    Mitchison, T.J.5
  • 15
    • 0032702259 scopus 로고    scopus 로고
    • Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins
    • Higgs H.N., Pollard T.D. Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins. J. Biol. Chem. 1999, 274:32531-32534.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32531-32534
    • Higgs, H.N.1    Pollard, T.D.2
  • 16
    • 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., Miki H., Suetsugu S., Ma L., Kirschner M.W., Takenawa T. 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 2000, 97:12631-12636.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12631-12636
    • Yamaguchi, H.1    Miki, H.2    Suetsugu, S.3    Ma, L.4    Kirschner, M.W.5    Takenawa, T.6
  • 17
    • 21544480823 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin
    • Clifton D.R., Dooley C.A., Grieshaber S.S., Carabeo R.A., Fields K.A., Hackstadt T. Tyrosine phosphorylation of the chlamydial effector protein Tarp is species specific and not required for recruitment of actin. Infect. Immun. 2005, 73:3860-3868.
    • (2005) Infect. Immun. , vol.73 , pp. 3860-3868
    • Clifton, D.R.1    Dooley, C.A.2    Grieshaber, S.S.3    Carabeo, R.A.4    Fields, K.A.5    Hackstadt, T.6
  • 19
    • 56649083314 scopus 로고    scopus 로고
    • Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation
    • Mehlitz A., Banhart S., Hess S., Selbach M., Meyer T.F. Complex kinase requirements for Chlamydia trachomatis Tarp phosphorylation. FEMS Microbiol. Lett. 2008, 289:233-240.
    • (2008) FEMS Microbiol. Lett. , vol.289 , pp. 233-240
    • Mehlitz, A.1    Banhart, S.2    Hess, S.3    Selbach, M.4    Meyer, T.F.5
  • 23
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann K.J., Pollard T.D. Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. USA 2001, 98:15009-15013.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 24
    • 0035094485 scopus 로고    scopus 로고
    • The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
    • Amann K.J., Pollard T.D. The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat. Cell. Biol. 2001, 3:306-310.
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 306-310
    • Amann, K.J.1    Pollard, T.D.2
  • 26
    • 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., Miura 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. 1996, 15:5326-5335.
    • (1996) EMBO J. , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 28
    • 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., Skoble J., Portnoy D.A., Mitchison T.J. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 1998, 281:105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 31
    • 80055088874 scopus 로고    scopus 로고
    • Chlamydia trachomatis Co-opts the FGF2 signaling pathway to enhance infection.
    • J.H. Kim, S. Jiang, C.A. Elwell, J.N. Engel, Chlamydia trachomatis Co-opts the FGF2 signaling pathway to enhance infection. PLoS Pathog 7 e1002285.
    • PLoS Pathog , vol.7
    • Kim, J.H.1    Jiang, S.2    Elwell, C.A.3    Engel, J.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.