메뉴 건너뛰기




Volumn 165, Issue 2, 2004, Pages 233-242

Fascin-mediated propulsion of Listeria monocytogenes independent of frequent nucleation by the Arp2/3 complex

Author keywords

Actin; Arp2 3; Fascin; Filopodia; Listeria

Indexed keywords

ACTIN RELATED PROTEIN 2; ACTIN RELATED PROTEIN 3; BRAIN EXTRACT; ELONGATION FACTOR; FASCIN; G ACTIN;

EID: 2142654946     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200311040     Document Type: Article
Times cited : (76)

References (45)
  • 4
    • 0025764370 scopus 로고
    • Purification of cap Z from chicken skeletal muscle
    • Casella, J.F., and J.A. Cooper. 1991. Purification of cap Z from chicken skeletal muscle. Methods Enzymol. 196:140-152.
    • (1991) Methods Enzymol. , vol.196 , pp. 140-152
    • Casella, J.F.1    Cooper, J.A.2
  • 5
    • 0025081821 scopus 로고
    • Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly
    • Dabiri, G.A., J.M. Sanger, D.A. Portnoy, and F.S. Southwick. 1990. Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly. Proc. Natl. Acad. Sci. USA. 87:6068-6072.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6068-6072
    • Dabiri, G.A.1    Sanger, J.M.2    Portnoy, D.A.3    Southwick, F.S.4
  • 6
    • 0035910044 scopus 로고    scopus 로고
    • Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments
    • Dayel, M.J., E.A. Holleran, and R.D. Mullins. 2001. Arp2/3 complex requires hydrolyzable ATP for nucleation of new actin filaments. Proc. Natl. Acad. Sci. USA. 98:14871-14876.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14871-14876
    • Dayel, M.J.1    Holleran, E.A.2    Mullins, R.D.3
  • 7
    • 0028237089 scopus 로고
    • Intact α-actinin molecules are needed for both the assembly of actin into the tails and the locomotion of Listeria monocytogenes inside infected cells
    • Dold, F.G., J.M. Sanger, and J.W. Sanger. 1994. Intact α-actinin molecules are needed for both the assembly of actin into the tails and the locomotion of Listeria monocytogenes inside infected cells. Cell Motil. Cytoskeleton. 28:97-107.
    • (1994) Cell Motil. Cytoskeleton. , vol.28 , pp. 97-107
    • Dold, F.G.1    Sanger, J.M.2    Sanger, J.W.3
  • 8
    • 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., T.P. Loisel, V. Laurent, R. Li, D. Pantaloni, P.J. Sansonetti, and M.F. Carlier. 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    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.F.7
  • 9
    • 0019320755 scopus 로고
    • A rapid purification of α-actinin, filamin, and a 130,000-dalton protein from smooth muscle
    • Feramisco, J.R., and K. Burridge. 1980. A rapid purification of α-actinin, filamin, and a 130,000-dalton protein from smooth muscle. J. Biol. Chem. 255: 1194-1199.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1194-1199
    • Feramisco, J.R.1    Burridge, K.2
  • 10
    • 0033747006 scopus 로고    scopus 로고
    • An elastic analysis of Listeria monocytogenes propulsion
    • Gerbal, F., P. Chaikin, Y. Rabin, and J. Prost. 2000. An elastic analysis of Listeria monocytogenes propulsion. Biophys. J. 79:2259-2275.
    • (2000) Biophys. J. , vol.79 , pp. 2259-2275
    • Gerbal, F.1    Chaikin, P.2    Rabin, Y.3    Prost, J.4
  • 11
    • 0038652046 scopus 로고    scopus 로고
    • Compression forces generated by actin comet tails on lipid vesicles
    • Giardini, P.A., D.A. Fletcher, and J.A. Theriot. 2003. Compression forces generated by actin comet tails on lipid vesicles. Proc. Natl. Acad. Sci. USA. 100: 6493-6498.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6493-6498
    • Giardini, P.A.1    Fletcher, D.A.2    Theriot, J.A.3
  • 12
    • 0023735811 scopus 로고
    • Behaviour of microtubules and actin filaments in living Drosophila embryos
    • Kellogg, D.R., T.J. Mitchison, and B.M. Alberts. 1988. Behaviour of microtubules and actin filaments in living Drosophila embryos. Development. 103:675-686.
    • (1988) Development , vol.103 , pp. 675-686
    • Kellogg, D.R.1    Mitchison, T.J.2    Alberts, B.M.3
  • 13
    • 0027817589 scopus 로고
    • Directional actin assembly by Listeria monocytogenes at the site of polar surface expression of the acta gene product involving the actin-bundling protein plastin (fimbrin)
    • Kocks, C., and P. Cossart. 1993. Directional actin assembly by Listeria monocytogenes at the site of polar surface expression of the acta gene product involving the actin-bundling protein plastin (fimbrin). Infect. Agents Dis. 2:207-209.
    • (1993) Infect. Agents Dis. , vol.2 , pp. 207-209
    • Kocks, C.1    Cossart, P.2
  • 14
    • 0026437563 scopus 로고
    • Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity
    • Lewis, A.K., and P.C. Bridgman. 1992. Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity. J. Cell Biol. 119:1219-1243.
    • (1992) J. Cell Biol. , vol.119 , pp. 1219-1243
    • Lewis, A.K.1    Bridgman, P.C.2
  • 15
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • Loisel, T.P., R. Boujemaa, D. Pantaloni, and M.F. Carlier. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature. 401: 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 16
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • Mallavarapu, A., and T. Mitchison. 1999. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell Biol. 146: 1097-1106.
    • (1999) J. Cell Biol. , vol.146 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 18
    • 0037447264 scopus 로고    scopus 로고
    • Listeria motility: Biophysics pushes things forward
    • Merz, A.J., and H.N. Higgs. 2003. Listeria motility: biophysics pushes things forward. Curr. Biol. 13:R302-R304.
    • (2003) Curr. Biol. , vol.13
    • Merz, A.J.1    Higgs, H.N.2
  • 19
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner, A., and G. Oster. 1996. Cell motility driven by actin polymerization. Biophys. J. 71:3030-3045.
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 20
    • 0037339268 scopus 로고    scopus 로고
    • Force generation by actin polymerization II: The elastic ratchet and tethered filaments
    • Mogilner, A., and G. Oster. 2003a. Force generation by actin polymerization II: the elastic ratchet and tethered filaments. Biophys. J. 84:1591-1605.
    • (2003) Biophys. J. , vol.84 , pp. 1591-1605
    • Mogilner, A.1    Oster, G.2
  • 21
    • 0141504153 scopus 로고    scopus 로고
    • Polymer motors: Pushing out the front and pulling up the back
    • Mogilner, A., and G. Oster. 2003b. Polymer motors: pushing out the front and pulling up the back. Curr. Biol. 13:R721-R733.
    • (2003) Curr. Biol. , vol.13
    • Mogilner, A.1    Oster, G.2
  • 22
    • 0034843552 scopus 로고    scopus 로고
    • Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake
    • Monack, D.M., and 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
  • 23
    • 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., J.A. Heuser, and T.D. Pollard. 1998. 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. 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
  • 24
  • 25
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., and G.G. Borisy. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 26
    • 0036327382 scopus 로고    scopus 로고
    • The cell biology of Listeria monocytogenes infection: The intersection of bacterial pathogenesis and cell-mediated immunity
    • Portnoy, D.A., V. Auerbuch, and I.J. Glomski. 2002. The cell biology of Listeria monocytogenes infection: the intersection of bacterial pathogenesis and cell-mediated immunity. J. Cell Biol. 158:409-414.
    • (2002) J. Cell Biol. , vol.158 , pp. 409-414
    • Portnoy, D.A.1    Auerbuch, V.2    Glomski, I.J.3
  • 27
    • 0030908903 scopus 로고    scopus 로고
    • The isolated comet tail pseudopodium of Listeria monocytogenes: A tail of two actin filament populations, long and axial and short and random
    • Sechi, A.S., J. Wehland, and J.V. Small. 1997. The isolated comet tail pseudopodium of Listeria monocytogenes: a tail of two actin filament populations, long and axial and short and random. J. Cell Biol. 137:155-167.
    • (1997) J. Cell Biol. , vol.137 , pp. 155-167
    • Sechi, A.S.1    Wehland, J.2    Small, J.V.3
  • 28
    • 0033515062 scopus 로고    scopus 로고
    • Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics
    • Selden, L.A., H.J. Kinosian, J.E. Estes, and L.C. Gershman. 1999. Impact of profilin on actin-bound nucleotide exchange and actin polymerization dynamics. Biochemistry. 38:2769-2778.
    • (1999) Biochemistry , vol.38 , pp. 2769-2778
    • Selden, L.A.1    Kinosian, H.J.2    Estes, J.E.3    Gershman, L.C.4
  • 29
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T.M., and G.G. Borisy. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 31
    • 0029776445 scopus 로고    scopus 로고
    • β-Catenin associates with the actin-bundling protein fascin in a noncadherin complex
    • Tao, Y.S., R.A. Edwards, B. Tubb, S. Wang, J. Bryan, and P.D. McCrea. 1996. β-Catenin associates with the actin-bundling protein fascin in a noncadherin complex. J. Cell Biol. 134:1271-1281.
    • (1996) J. Cell Biol. , vol.134 , pp. 1271-1281
    • Tao, Y.S.1    Edwards, R.A.2    Tubb, B.3    Wang, S.4    Bryan, J.5    McCrea, P.D.6
  • 33
    • 0025740949 scopus 로고
    • Actin microfilament dynamics in locomoting cells
    • Theriot, J.A., and T.J. Mitchison. 1991. Actin microfilament dynamics in locomoting cells. Nature. 352:126-131.
    • (1991) Nature , vol.352 , pp. 126-131
    • Theriot, J.A.1    Mitchison, T.J.2
  • 34
    • 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, and 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
  • 35
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney, L.G., and D.A. Portnoy. 1989. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J. Cell Biol. 109:1597-1608.
    • (1989) J. Cell Biol. , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 36
    • 0026659493 scopus 로고
    • How Listeria exploits host cell actin to form its own cytoskeleton. 11. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper
    • Tilney, L.G., D.J. DeRosier, A. Weber, and M.S. Tilney. 1992, How Listeria exploits host cell actin to form its own cytoskeleton. 11. Nucleation, actin filament polarity, filament assembly, and evidence for a pointed end capper. J. Cell Biol. 118:83-93.
    • (1992) J. Cell Biol. , vol.118 , pp. 83-93
    • Tilney, L.G.1    DeRosier, D.J.2    Weber, A.3    Tilney, M.S.4
  • 37
    • 0141838877 scopus 로고    scopus 로고
    • Biomimetic systems for studying actin-based motility
    • Upadhyaya, A., and A. van Oudenaarden. 2003. Biomimetic systems for studying actin-based motility. Curr. Biol. 13:R734-R744.
    • (2003) Curr. Biol. , vol.13
    • Upadhyaya, A.1    Van Oudenaarden, A.2
  • 40
    • 0031610209 scopus 로고    scopus 로고
    • Purification and assay of the platelet Arp2/3 complex
    • Welch, M.D., and T.J. Mitchison. 1998. Purification and assay of the platelet Arp2/3 complex. Methods Enzymol. 298:52-61.
    • (1998) Methods Enzymol. , vol.298 , pp. 52-61
    • Welch, M.D.1    Mitchison, T.J.2
  • 41
    • 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, and 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
  • 43
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • Yarar, D., W. To, A. Abo, and M.D. Welch. 1999. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9:555-558.
    • (1999) Curr. Biol. , vol.9 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4
  • 44
    • 0035793587 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 complex
    • Zalevsky, J., I. Grigorova, and R.D. Mullins. 2001. Activation of the Arp2/3 complex by the Listeria acta protein. Acta binds two actin monomers and three subunits of the Arp2/3 complex. J. Biol. Chem. 276:3468-3475.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3468-3475
    • Zalevsky, J.1    Grigorova, I.2    Mullins, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.