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Volumn 72, Issue 11, 1998, Pages 8806-8812

Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by rho family GTPases

Author keywords

[No Author keywords available]

Indexed keywords

CLOSTRIDIUM TOXIN; CYTOCHALASIN D; GUANOSINE TRIPHOSPHATASE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 HYDROXYKINASE; PHOSPHATIDYLINOSITOL 3 KINASE; RAS PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA;

EID: 0031663239     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.11.8806-8812.1998     Document Type: Article
Times cited : (203)

References (57)
  • 2
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., B. Derijard, R. J. Davis, and R. A. Cerione. 1995. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J. Biol. Chem. 270:27995-27998.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 5
    • 0030948670 scopus 로고    scopus 로고
    • Gene therapy: Progress, problems, prospects
    • Blau, H., and P. Khavari. 1997. Gene therapy: progress, problems, prospects. Nat. Med. 3:612-613.
    • (1997) Nat. Med. , vol.3 , pp. 612-613
    • Blau, H.1    Khavari, P.2
  • 7
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., D. Drechsel, and D. Hall. 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, D.3
  • 8
    • 0028915743 scopus 로고
    • GTPase cascades choreographing cellular behavior: Movement, morphogenesis and more
    • Chant, J., and L. Stowers. 1995. GTPase cascades choreographing cellular behavior: movement, morphogenesis and more. Cell 81:1-4.
    • (1995) Cell , vol.81 , pp. 1-4
    • Chant, J.1    Stowers, L.2
  • 9
    • 0014748494 scopus 로고
    • Early events in the interaction of adenoviruses with HeLa cells. I. Penetration of type 5 and intracellular release of the DNA genome
    • Chardonnet, Y., and S. Dales. 1970. Early events in the interaction of adenoviruses with HeLa cells. I. Penetration of type 5 and intracellular release of the DNA genome. Virology 40:462-477.
    • (1970) Virology , vol.40 , pp. 462-477
    • Chardonnet, Y.1    Dales, S.2
  • 10
    • 0030448437 scopus 로고    scopus 로고
    • Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses
    • Chen, L.-M., S. Hobbie, and J. E. Galan. 1996. Requirement of CDC42 for Salmonella-induced cytoskeletal and nuclear responses. Science 274:2115-2118.
    • (1996) Science , vol.274 , pp. 2115-2118
    • Chen, L.-M.1    Hobbie, S.2    Galan, J.E.3
  • 11
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 13
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O. A., M. Chiariello, J.-C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J. S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.-C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 14
    • 0030772657 scopus 로고    scopus 로고
    • Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells
    • Dharmawhardane, S., L. C. Sanders, S. S. Martin, R. H. Daniels, and G. M. Bokoch. 1997. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol. 138: 1265-1278.
    • (1997) J. Cell Biol. , vol.138 , pp. 1265-1278
    • Dharmawhardane, S.1    Sanders, L.C.2    Martin, S.S.3    Daniels, R.H.4    Bokoch, G.M.5
  • 15
    • 0029780095 scopus 로고    scopus 로고
    • The renaturable 69- and 63-kDa protein kinases that undergo rapid activation in chemoattractant-stimulated guinea pig neutrophils are p21-activated kinases
    • Ding, J., U. G. Knaus, J. P. Lian, G. M. Bokoch, and J. A. Badwey. 1996. The renaturable 69- and 63-kDa protein kinases that undergo rapid activation in chemoattractant-stimulated guinea pig neutrophils are p21-activated kinases. J. Biol. Chem. 271:24869-24873.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24869-24873
    • Ding, J.1    Knaus, U.G.2    Lian, J.P.3    Bokoch, G.M.4    Badwey, J.A.5
  • 16
    • 0017336387 scopus 로고
    • Synthesis and processing of the precursor to the major core protein of adenovirus type 2
    • Everitt, E., S. A. Meador, and A. S. Levine. 1977. Synthesis and processing of the precursor to the major core protein of adenovirus type 2. J. Virol. 21:199-214.
    • (1977) J. Virol. , vol.21 , pp. 199-214
    • Everitt, E.1    Meador, S.A.2    Levine, A.S.3
  • 17
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 18
    • 0027469161 scopus 로고
    • Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells
    • Gottlieb, T. A., I. E. Ivanov, M. Adesnik, and D. D. Sabatini. 1993. Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells. J. Cell Biol. 120:695-709.
    • (1993) J. Cell Biol. , vol.120 , pp. 695-709
    • Gottlieb, T.A.1    Ivanov, I.E.2    Adesnik, M.3    Sabatini, D.D.4
  • 19
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 21
    • 0003354726 scopus 로고    scopus 로고
    • Adenovirus
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Horwitz, M. S. 1996. Adenovirus, p. 2149-2171. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 2149-2171
    • Horwitz, M.S.1
  • 22
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho/Rac GTPases
    • Hotchin, N., and A. Hall. 1995. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho/Rac GTPases. J. Cell Biol. 131:1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.1    Hall, A.2
  • 23
    • 0029855239 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases
    • Hotchin, N. A., and A. Hall. 1996. Regulation of the actin cytoskeleton, integrins and cell growth by the Rho family of small GTPases. Cancer Surv. 27:311-322.
    • (1996) Cancer Surv. , vol.27 , pp. 311-322
    • Hotchin, N.A.1    Hall, A.2
  • 24
    • 0029802561 scopus 로고    scopus 로고
    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Joneson, T., M. McDonough, D. Bar-Sagi, and L. Aelst. 1998. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science 274:1374-1378.
    • (1998) Science , vol.274 , pp. 1374-1378
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, D.3    Aelst, L.4
  • 26
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5,-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Karlund, J. K., A. Guilherme, J. J. Holik, J. V. Virbasius, A. Chawla, and M. P. Czech. 1997. Signaling by phosphoinositide-3,4,5,-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275:1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Karlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 27
    • 0032489531 scopus 로고    scopus 로고
    • Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase
    • Kimura, K., Y. Fukata, Y. Matsuoka, V. Bennett, Y. Matsuura, K. Okawa, A. Iwamatsu, and K. Kaibuchi. 1998. Regulation of the association of adducin with actin filaments by Rho-associated kinase (Rho-kinase) and myosin phosphatase. J. Biol. Chem. 273:5542-5548.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5542-5548
    • Kimura, K.1    Fukata, Y.2    Matsuoka, Y.3    Bennett, V.4    Matsuura, Y.5    Okawa, K.6    Iwamatsu, A.7    Kaibuchi, K.8
  • 29
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze, C., L. M. Fujimoto, H. L. Yin, and S. L. Schmid. 1997. The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem. 272:20332-20335.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 31
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the Rac GTPase on purkinje cell axons and dendritic trunks and spines
    • Luo, L., T. K. Hensch, L. Ackerman, S. Barbel, L. Y. Jan, and Y. N. Jan. 1996. Differential effects of the Rac GTPase on purkinje cell axons and dendritic trunks and spines. Nature 379:837-840.
    • (1996) Nature , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 32
    • 0028086441 scopus 로고
    • Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion
    • Luo, L., J. Liao, L. Y. Jan, and Y. N. Jan. 1994. Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion. Genes Dev. 8:1787-1802.
    • (1994) Genes Dev. , vol.8 , pp. 1787-1802
    • Luo, L.1    Liao, J.2    Jan, L.Y.3    Jan, Y.N.4
  • 33
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., T. Leung, H. Salihuddin, Z. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367: 40-46.
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 34
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F. X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 35
    • 0029959468 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau, V., A. Madania, R. P. Martin, and B. Winsor. 1996. The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134:117-132.
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.P.3    Winsor, B.4
  • 36
    • 0028204439 scopus 로고
    • Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane
    • Mulholland, J., D. Preuss, A. Moon, A. Wong, D. Drubin, and D. Botstein. 1994. Ultrastructure of the yeast actin cytoskeleton and its association with the plasma membrane. J. Cell Biol. 125:381-391.
    • (1994) J. Cell Biol. , vol.125 , pp. 381-391
    • Mulholland, J.1    Preuss, D.2    Moon, A.3    Wong, A.4    Drubin, D.5    Botstein, D.6
  • 37
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 38
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors
    • Nobes, C. D., P. Hawkins, L. Stephens, and A. Hall. 1995. Activation of the small GTP-binding proteins Rho and Rac by growth factor receptors. J. Cell Science 108:225-233.
    • (1995) J. Cell Science , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 39
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signaling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parsons, J. T. 1996. Integrin-mediated signaling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr. Opin. Cell Biol. 8:146-152.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 146-152
    • Parsons, J.T.1
  • 40
    • 0020615118 scopus 로고
    • Ultrastructural and immunofluorescence studies of early events in adenovirus-HeLa cell interactions
    • Patterson, S., and W. C. Russell. 1983. Ultrastructural and immunofluorescence studies of early events in adenovirus-HeLa cell interactions. J. Gen. Virol. 64:1091-1099.
    • (1983) J. Gen. Virol. , vol.64 , pp. 1091-1099
    • Patterson, S.1    Russell, W.C.2
  • 41
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 43
    • 0343907239 scopus 로고    scopus 로고
    • Is dynamin really a 'pinchase'?
    • Roos, J., and R. B. Kelly. 1997. Is dynamin really a 'pinchase'? Trends Cell Biol. 7:257-259.
    • (1997) Trends Cell Biol. , vol.7 , pp. 257-259
    • Roos, J.1    Kelly, R.B.2
  • 44
    • 0031127255 scopus 로고    scopus 로고
    • Emerging from the Pak: The p21-activated protein kinase family
    • Sells, M. A., and J. Chernoff. 1997. Emerging from the Pak: the p21-activated protein kinase family. Trends Cell Biol. 7:162-167.
    • (1997) Trends Cell Biol. , vol.7 , pp. 162-167
    • Sells, M.A.1    Chernoff, J.2
  • 45
  • 47
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin
    • Tapon, N., and A. Hall. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin. Curr. Opin. Cell Biol. 9:86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 48
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias, K. F., L. Cantley, and C. L. Carpenter. 1995. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270:17656-17659.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.2    Carpenter, C.L.3
  • 49
    • 0031950120 scopus 로고    scopus 로고
    • Adenovirus internalization and infection require dynamin
    • Wang, K., S. Huang, A. Kapoor-Munshi, and G. Nemerow. 1998. Adenovirus internalization and infection require dynamin. J. Virol. 72:3455-3458.
    • (1998) J. Virol. , vol.72 , pp. 3455-3458
    • Wang, K.1    Huang, S.2    Kapoor-Munshi, A.3    Nemerow, G.4
  • 51
    • 0030563195 scopus 로고    scopus 로고
    • Adenoviruses as gene-delivery vehicles
    • Wilson, J. M. 1996. Adenoviruses as gene-delivery vehicles. N. Engl. J. Med. 334:1185-1187.
    • (1996) N. Engl. J. Med. , vol.334 , pp. 1185-1187
    • Wilson, J.M.1
  • 52
    • 0002847802 scopus 로고
    • Introduction and overview
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Wimmer, E. (ed.). 1994. Introduction and overview, p. 1-13. In Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 1-13
    • Wimmer, E.1
  • 53
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke, W., A. V. Podtelejnikov, A. DiNardo, J. D. Sutherland, C. B. Gurniak, C. Dotti, and M. Mann. 1998. In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17:967-976.
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    DiNardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5    Dotti, C.6    Mann, M.7
  • 54
    • 0030983936 scopus 로고    scopus 로고
    • Lack of high affinity fiber receptor activity explains the resistance of ciliated airway epithelia to adenovirus infection
    • Zabner, J., P. Freimuth, A. Puga, A. Fabrega, and M. J. Welsh. 1997. Lack of high affinity fiber receptor activity explains the resistance of ciliated airway epithelia to adenovirus infection. J. Clin. Invest. 100:1144-1149.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1144-1149
    • Zabner, J.1    Freimuth, P.2    Puga, A.3    Fabrega, A.4    Welsh, M.J.5
  • 55
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang, S., J. Han, M. A. Sells, J. Chernoff, U. G. Knaus, R. J. Ulevitch, and G. M. Bokoch. 1995. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J. Biol. Chem. 270: 23934-23936.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 56
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng, Y., S. Bagrodia, and R. A. Cerione. 1994. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269:18727-18730.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 57
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond, S. H. 1996. Signal transduction and actin filament organization. Curr. Biol. 8:66-73.
    • (1996) Curr. Biol. , vol.8 , pp. 66-73
    • Zigmond, S.H.1


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