메뉴 건너뛰기




Volumn 66, Issue 8, 1998, Pages 3775-3782

Gelsolin, a protein that caps the barbed ends and severs actin filaments, enhances the actin-based motility of Listeria monocytogenes in host cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GELSOLIN; REGULATOR PROTEIN;

EID: 0031848173     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.66.8.3775-3782.1998     Document Type: Article
Times cited : (23)

References (36)
  • 1
    • 0028603483 scopus 로고
    • Gelsolin displaces phalloidin from actin filaments. A new fluorescence method shows that both Ca2+ and Mg2+ affect the rate at which gelsolin severs F-actin
    • Allen, P. G., and P. A. Janmey. 1994. Gelsolin displaces phalloidin from actin filaments. A new fluorescence method shows that both Ca2+ and Mg2+ affect the rate at which gelsolin severs F-actin. J. Biol. Chem. 269:32916-32923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 2
    • 0020825184 scopus 로고
    • Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament
    • Bonder, E. M., D. J. Fishkind, and M. S. Mooseker. 1983. Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament. Cell 34:491-501.
    • (1983) Cell , vol.34 , pp. 491-501
    • Bonder, E.M.1    Fishkind, D.J.2    Mooseker, M.S.3
  • 3
  • 4
    • 0028933782 scopus 로고
    • A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin-based cytoskeleton of mammalian cells
    • Charkraborty, T., F. Ebel, E. Domann, K. Niebuhr, B. Gerstel, S. Pistor, C. J. Temm-Grove, B. M. Jockusch, M. Reinhard, U. Walter, and J. Wehland. 1995. 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) EMBO J. , vol.14 , pp. 1314-1321
    • Charkraborty, T.1    Ebel, F.2    Domann, E.3    Niebuhr, K.4    Gerstel, B.5    Pistor, S.6    Temm-Grove, C.J.7    Jockusch, B.M.8    Reinhard, M.9    Walter, U.10    Wehland, J.11
  • 5
    • 0025782925 scopus 로고
    • Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin
    • Cunningham, C. C., T. P. Stossel, and D. J. Kwiatkowski. 1991. Enhanced motility in NIH 3T3 fibroblasts that overexpress gelsolin. Science 251:1233-1236.
    • (1991) Science , vol.251 , pp. 1233-1236
    • Cunningham, C.C.1    Stossel, T.P.2    Kwiatkowski, D.J.3
  • 6
    • 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
  • 7
    • 0026768703 scopus 로고
    • Molecular cloning of human macrophage capping protein cDNA: A unique member of the gelsolin/villin family expressed primarily in macrophages
    • Dabiri, G. A., C. L. Young, J. Rosenbloom, and F. S. Southwick. 1992. Molecular cloning of human macrophage capping protein cDNA: a unique member of the gelsolin/villin family expressed primarily in macrophages. J. Biol. Chem. 267:16545-16552.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16545-16552
    • Dabiri, G.A.1    Young, C.L.2    Rosenbloom, J.3    Southwick, F.S.4
  • 8
    • 0029918141 scopus 로고    scopus 로고
    • Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity
    • Dabrowska, R., H. Hinssen, B. Galazkiewicz, and E. Nowak. 1996. Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity. Biochem. J. 315:753-759.
    • (1996) Biochem. J. , vol.315 , pp. 753-759
    • Dabrowska, R.1    Hinssen, H.2    Galazkiewicz, B.3    Nowak, E.4
  • 9
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family
    • Dramsi, S., I. Biswas, E. Maguin, L. Braun, P. Mastroeni, and P. Cossart. 1995. Entry of Listeria monocytogenes into hepatocytes requires expression of InlB, a surface protein of the internalin multigene family. Mol. Microbiol. 16: 251-261.
    • (1995) Mol. Microbiol. , vol.16 , pp. 251-261
    • Dramsi, S.1    Biswas, I.2    Maguin, E.3    Braun, L.4    Mastroeni, P.5    Cossart, P.6
  • 10
    • 0020600552 scopus 로고
    • Isolation and some structural and functional properties of macrophage tropomyosin
    • Fattoum, A., J. H. Hartwig, and T. P. Stossel. 1983. Isolation and some structural and functional properties of macrophage tropomyosin. Biochemistry 22:1187-1193.
    • (1983) Biochemistry , vol.22 , pp. 1187-1193
    • Fattoum, A.1    Hartwig, J.H.2    Stossel, T.P.3
  • 11
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of the surface antigens from Gram-positive cocci
    • Gaillard, J.-L., P. Berche, C. Frehel, E. Gouin, and P. Cossart. 1991. Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of the surface antigens from Gram-positive cocci. Cell 65:1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.-L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 13
    • 0030851599 scopus 로고    scopus 로고
    • Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): Implications for actin-based Listeria motility
    • Kang, F., R. O. Laine, M. R. Bubb, F. S. Southwick, and D. L. Purich. 1997. Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility. Biochemistry 36:8384-8392.
    • (1997) Biochemistry , vol.36 , pp. 8384-8392
    • Kang, F.1    Laine, R.O.2    Bubb, M.R.3    Southwick, F.S.4    Purich, D.L.5
  • 14
    • 0023138737 scopus 로고
    • Tn916-induced mutation in the hemolysin determinant affecting virulence of Listeria monocytogenes
    • Kathariou, S., P. Metz, H. Hof, and W. Goebel. 1987. Tn916-induced mutation in the hemolysin determinant affecting virulence of Listeria monocytogenes. J. Bacteriol. 169:1291-1297.
    • (1987) J. Bacteriol. , vol.169 , pp. 1291-1297
    • Kathariou, S.1    Metz, P.2    Hof, H.3    Goebel, W.4
  • 15
    • 0027941774 scopus 로고
    • Role of T cell subsets in immunity against intracellular bacteria: Experimental infections of knock-out mice with Listeria monocytogenes and Mycobacterium bovis BCG
    • Kaufmann, S. H., and C. H. Ladel. 1994. Role of T cell subsets in immunity against intracellular bacteria: experimental infections of knock-out mice with Listeria monocytogenes and Mycobacterium bovis BCG. Immunobiology 191:509-519.
    • (1994) Immunobiology , vol.191 , pp. 509-519
    • Kaufmann, S.H.1    Ladel, C.H.2
  • 16
    • 0028981496 scopus 로고
    • Actin-based movement of Listeria monocytogenes: Actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface
    • Marchand, J. B., P. Moreau, A. Paoletti, P. Cossart, M. F. Carlier, and D. Pantaloni. 1995. Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface. J. Cell Biol. 130:331-343.
    • (1995) J. Cell Biol. , vol.130 , pp. 331-343
    • Marchand, J.B.1    Moreau, P.2    Paoletti, A.3    Cossart, P.4    Carlier, M.F.5    Pantaloni, D.6
  • 17
    • 0027194759 scopus 로고
    • Cellular motions and thermal fluctuations: The Brownian ratchet
    • Peskin, C. S., G. M. Odell, and G. F. Oster. 1993. Cellular motions and thermal fluctuations: the Brownian ratchet. Biophys. J. 65:316-324.
    • (1993) Biophys. J. , vol.65 , pp. 316-324
    • Peskin, C.S.1    Odell, G.M.2    Oster, G.F.3
  • 18
    • 0019495845 scopus 로고
    • Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores
    • Pollard, T. D., and M. S. Mooseker. 1981. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J. Cell Biol. 88:654-659.
    • (1981) J. Cell Biol. , vol.88 , pp. 654-659
    • Pollard, T.D.1    Mooseker, M.S.2
  • 19
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy, D. A., P. S. Jacks, and D. J. Hinrichs. 1988. Role of hemolysin for the intracellular growth of Listeria monocytogenes. J. Exp. Med. 167:1459-1471.
    • (1988) J. Exp. Med. , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 20
    • 0030821155 scopus 로고    scopus 로고
    • Xenopus actin depolymerization factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails
    • Rosenblatt, J., B. J. Agnew, H. Abe, J. R. Bamburg, and T. J. Mitchison. 1997. Xenopus actin depolymerization factor/cofilin (XAC) is responsible for the turnover of actin filaments in Listeria monocytogenes tails. J. Cell Biol. 136:1323-1332.
    • (1997) J. Cell Biol. , vol.136 , pp. 1323-1332
    • Rosenblatt, J.1    Agnew, B.J.2    Abe, H.3    Bamburg, J.R.4    Mitchison, T.J.5
  • 21
    • 0026663057 scopus 로고
    • Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes
    • Sanger, J. M., J. W. Sanger, and F. S. Southwick. 1992. Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes. Infect. Immun. 60:3609-3619.
    • (1992) Infect. Immun. , vol.60 , pp. 3609-3619
    • Sanger, J.M.1    Sanger, J.W.2    Southwick, F.S.3
  • 22
    • 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
  • 23
    • 0028839091 scopus 로고
    • Gain-of-function mutations conferring actin-severing activity to human macrophage Cap G
    • Southwick, F. S. 1495. Gain-of-function mutations conferring actin-severing activity to human macrophage Cap G. J. Biol. Chem. 270:45-48.
    • (1495) J. Biol. Chem. , vol.270 , pp. 45-48
    • Southwick, F.S.1
  • 24
    • 0022974680 scopus 로고
    • Rabbit alveolar macrophages contain a Ca2+-sensitive, 41,000 dalton protein which reversibly blocks the "barbed" ends of actin filaments but does not sever them
    • Southwick, F. S., and M. J. DiNubile. 1986. Rabbit alveolar macrophages contain a Ca2+-sensitive, 41,000 dalton protein which reversibly blocks the "barbed" ends of actin filaments but does not sever them. J. Biol. Chem. 261: 14191-14195.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14191-14195
    • Southwick, F.S.1    DiNubile, M.J.2
  • 25
    • 0028276812 scopus 로고
    • Arrest of Listeria movement in host cells by a bacterial Acta analogue: Implications for actin-based motility
    • Southwick, F. S., and D. L. Purich. 1994. Arrest of Listeria movement in host cells by a bacterial ActA analogue: implications for actin-based motility. Proc. Natl. Acad. Sci. USA 91:5168-5172.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5168-5172
    • Southwick, F.S.1    Purich, D.L.2
  • 26
    • 0029870228 scopus 로고    scopus 로고
    • Mechanisms of disease: Intracellular pathogenesis of listeriosis
    • Southwick, F. S., and D. L. Purich. 1996. Mechanisms of disease: intracellular pathogenesis of listeriosis. N. Engl. J. Med. 334:770-776.
    • (1996) N. Engl. J. Med. , vol.334 , pp. 770-776
    • Southwick, F.S.1    Purich, D.L.2
  • 27
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 28
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel, T. P. 1993. On the crawling of animal cells. Science 260:1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 29
    • 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
  • 30
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts
    • Theriot, J. A., J. Rosenblatt, D. A. Portnoy, P. J. Goldschmidt-Clermont, and T. J. Mitchison. 1994. Involvement of profilin in the actin-based motility of L. monocytogenes in cells and in cell-free extracts. Cell 76:505-517.
    • (1994) Cell , vol.76 , pp. 505-517
    • Theriot, J.A.1    Rosenblatt, J.2    Portnoy, D.A.3    Goldschmidt-Clermont, P.J.4    Mitchison, T.J.5
  • 31
    • 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
  • 32
    • 0024318706 scopus 로고
    • Expression of human gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way, M., J. Gooch, B. Pope, and A. G. Weeds. 1989. Expression of human gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109:593-605.
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 33
    • 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
  • 34
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke, W., A. H. Sharpe, J. H. Hartwig, T. Azuma, T. P. Stossel, and D. J. Kwiatkowski. 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell 81:41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 35
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin, H. L., and T. P. Stossel. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature 281:583-586.
    • (1979) Nature , vol.281 , pp. 583-586
    • Yin, H.L.1    Stossel, T.P.2
  • 36
    • 0028214155 scopus 로고
    • Calcium regulation of actin filament capping and monomer binding by macrophage capping protein
    • Young, C. L., A. Feierstein, and F. S. Southwick. 1994. Calcium regulation of actin filament capping and monomer binding by macrophage capping protein. J. Biol. Chem. 269:13997-14002.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13997-14002
    • Young, C.L.1    Feierstein, A.2    Southwick, F.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.