메뉴 건너뛰기




Volumn 427, Issue 6973, 2004, Pages 457-461

The RickA protein of Rickettsia conorii activates the Arp2/3 complex

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; CELLS; POLYMERIZATION;

EID: 0842263990     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02318     Document Type: Article
Times cited : (225)

References (29)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465 (2003).
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht, F. & Way, M. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11, 30-38 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 3
    • 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 281, 105-108 (1998).
    • (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
  • 4
    • 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. 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).
    • (1999) J. Cell Sci. , vol.112 , pp. 1697-1708
    • Gouin, E.1
  • 5
    • 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. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl Acad. Sci. USA 96, 3739-3744 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3739-3744
    • Machesky, L.M.1
  • 6
    • 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. Listeria protein ActA mimics WASp family proteins: it activates filament barbed end branching by Arp2/3 complex. Biochemistry 40, 11390-11404 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11390-11404
    • Boujemaa-Paterski, R.1
  • 7
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel, T. P., Boujemaa, R., Pantaloni, D. & Carlier, M. F. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature 401, 613-616 (1999).
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 8
    • 0033565599 scopus 로고    scopus 로고
    • The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes
    • May, R. C. et al. The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes. Curr. Biol. 9, 759-762 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 759-762
    • May, R.C.1
  • 9
    • 0033528995 scopus 로고    scopus 로고
    • Activation of the yeast Arp2/3 complex by Beelp, a WASP-family protein
    • Winter, D., Lechler, T. & Li, R. Activation of the yeast Arp2/3 complex by Beelp, a WASP-family protein. Curr. Biol. 9, 501-504 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 501-504
    • Winter, D.1    Lechler, T.2    Li, R.3
  • 10
    • 0035814938 scopus 로고    scopus 로고
    • Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation
    • Weaver, A. M. et al. Cortactin promotes and stabilizes Arp2/3-induced actin filament network formation. Curr. Biol. 11, 370-374 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 370-374
    • Weaver, A.M.1
  • 11
    • 0035090317 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-mediated actin polymerization by cortactin
    • Uruno, T. et al. Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nature Cell Biol. 3, 259-266 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 259-266
    • Uruno, T.1
  • 12
    • 0345146913 scopus 로고    scopus 로고
    • Formation of filopodia-like bundles in vitro from a dendritic network
    • Vignjevic, D. et al. Formation of filopodia-like bundles in vitro from a dendritic network. J. Cell Biol. 160, 951-962 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 951-962
    • Vignjevic, D.1
  • 13
    • 0029929213 scopus 로고    scopus 로고
    • The biology of Rickettsiae
    • Hackstadt, T. The biology of Rickettsiae. Infect. Agents Dis. 5, 127-143 (1996).
    • (1996) Infect. Agents Dis. , vol.5 , pp. 127-143
    • Hackstadt, T.1
  • 14
    • 0027086804 scopus 로고
    • Intracellular movements of Rickettsia conorii and R. typhi based on actin polymerization
    • Teysseire, N., Chiche-Portiche, C. & Raoult, D. Intracellular movements of Rickettsia conorii and R. typhi based on actin polymerization. Res. Microbiol. 143, 821-829 (1992).
    • (1992) Res. Microbiol. , vol.143 , pp. 821-829
    • Teysseire, N.1    Chiche-Portiche, C.2    Raoult, D.3
  • 15
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekii and the origin of mitochondria
    • Andersson, S. G. et al. The genome sequence of Rickettsia prowazekii and the origin of mitochondria. Nature 396, 133-140 (1998).
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.1
  • 16
    • 0035860458 scopus 로고    scopus 로고
    • Mechanisms of evolution in Rickettsia conorii and R. prowazekii
    • Ogata, H. et al. Mechanisms of evolution in Rickettsia conorii and R. prowazekii. Science 293, 2093-2098 (2001).
    • (2001) Science , vol.293 , pp. 2093-2098
    • Ogata, H.1
  • 17
    • 0030060424 scopus 로고    scopus 로고
    • The actin binding site of thymosin beta 4 mapped by mutational analysis
    • Van Troys, M. et al. The actin binding site of thymosin beta 4 mapped by mutational analysis. EMBO J. 15, 201-210 (1996).
    • (1996) EMBO J. , vol.15 , pp. 201-210
    • Van Troys, M.1
  • 18
    • 0041989754 scopus 로고    scopus 로고
    • A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
    • Panchal, S. C., Kaiser, D. A., Torres, E., Pollard, T. D. & Rosen, M. K. A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex. Nature Struct. Biol. 10, 591-598 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 591-598
    • Panchal, S.C.1    Kaiser, D.A.2    Torres, E.3    Pollard, T.D.4    Rosen, M.K.5
  • 19
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin, L. et al. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007-1011 (2000).
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1
  • 20
    • 0033914895 scopus 로고    scopus 로고
    • Ultrastructure of Rickettsia ricketzsii actin tails and localization of cytoskeletal proteins
    • Van Kirk, L. S., Hayes, S. F. & Heinzen, R. A. Ultrastructure of Rickettsia ricketzsii actin tails and localization of cytoskeletal proteins. Infect. Immun. 68, 4706-4713 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 4706-4713
    • Van Kirk, L.S.1    Hayes, S.F.2    Heinzen, R.A.3
  • 21
    • 0029079119 scopus 로고
    • Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function
    • Friederich, E. et al. Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function. EMBO J. 14, 2731-2744 (1995).
    • (1995) EMBO J. , vol.14 , pp. 2731-2744
    • Friederich, E.1
  • 23
    • 0028933782 scopus 로고
    • A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells
    • Chakraborty, T. et al. A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells. EMBO J. 14, 1314-1321 (1995).
    • (1995) EMBO J. , vol.14 , pp. 1314-1321
    • Chakraborty, T.1
  • 24
    • 0034705317 scopus 로고    scopus 로고
    • Negative regulation of fibroblast motility by Ena/VASP proteins
    • Bear, J. E. et al. Negative regulation of fibroblast motility by Ena/ VASP proteins. Cell 101, 717-728 (2000).
    • (2000) Cell , vol.101 , pp. 717-728
    • Bear, J.E.1
  • 25
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • Bear, J. E. et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell 109, 509-521 (2002).
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1
  • 26
    • 0035494440 scopus 로고    scopus 로고
    • Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility
    • Skoble, J. et al. Pivotal role of VASP in Arp2/3 complex-mediated actin nucleation, actin branch-formation, and Listeria monocytogenes motility. J. Cell Biol. 155, 89-100 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 89-100
    • Skoble, J.1
  • 27
    • 0038392873 scopus 로고    scopus 로고
    • Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP
    • Cory, G. O., Cramer, R., Blanchoin, L. & Ridley, A. J. Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol. Cell 11, 1229-1239 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1229-1239
    • Cory, G.O.1    Cramer, R.2    Blanchoin, L.3    Ridley, A.J.4
  • 28
    • 0029796520 scopus 로고    scopus 로고
    • Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: Higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity
    • Lamarche, N. et al. Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity. Biochem. J. 320, 129-135 (1996).
    • (1996) Biochem. J. , vol.320 , pp. 129-135
    • Lamarche, N.1
  • 29
    • 0031731076 scopus 로고    scopus 로고
    • Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach
    • David, V. et al. Identification of cofilin, coronin, Rac and capZ in actin tails using a Listeria affinity approach. J. Cell Sci. 111, 2877-2884 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 2877-2884
    • David, V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.