메뉴 건너뛰기




Volumn 79, Issue 18, 2005, Pages 11766-11775

Vimentin rearrangement during African swine fever virus infection involves retrograde transport along microtubules and phosphorylation of vimentin by calcium calmodulin kinase II

Author keywords

[No Author keywords available]

Indexed keywords

N [2 [[N [3 (4 CHLOROPHENYL) 2 PROPENYL] N METHYLAMINO]METHYL]PHENYL] N (2 HYDROXYETHYL) 4 METHOXYBENZENESULFONAMIDE; PROTEIN KINASE (CALCIUM,CALMODULIN) II; SERINE; VIMENTIN; VIRUS DNA;

EID: 24644480042     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.18.11766-11775.2005     Document Type: Article
Times cited : (107)

References (50)
  • 1
    • 0026719687 scopus 로고
    • Characterization of p-30, a highly antigenic membrane and secreted protein of African swine fever virus
    • Afonso, C. L., C. Alcaraz, A. Brun, M. D. Sussman, D. V. Onisk, J. M. Escribano, and D. L. Rock. 1992. Characterization of p-30, a highly antigenic membrane and secreted protein of African swine fever virus. Virology 189:368-373.
    • (1992) Virology , vol.189 , pp. 368-373
    • Afonso, C.L.1    Alcaraz, C.2    Brun, A.3    Sussman, M.D.4    Onisk, D.V.5    Escribano, J.M.6    Rock, D.L.7
  • 2
    • 0024512061 scopus 로고
    • Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
    • Ando, S., K. Tanabe, Y. Gonda, C. Sato, and M. Inagaki. 1989. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28:2974-2979.
    • (1989) Biochemistry , vol.28 , pp. 2974-2979
    • Ando, S.1    Tanabe, K.2    Gonda, Y.3    Sato, C.4    Inagaki, M.5
  • 4
    • 0031711867 scopus 로고    scopus 로고
    • African swine fever virus is enveloped by a two-membraned collapsed cis-terna derived from the endoplasmic reticulum
    • Andres, G., R. Garcia-Escudero, C. Simon-Mateo, and E. Vinuela. 1998. African swine fever virus is enveloped by a two-membraned collapsed cis-terna derived from the endoplasmic reticulum. J. Virol. 72:8988-9001.
    • (1998) J. Virol. , vol.72 , pp. 8988-9001
    • Andres, G.1    Garcia-Escudero, R.2    Simon-Mateo, C.3    Vinuela, E.4
  • 5
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., S. Mitra, E. S. Schweitzer, M. R. Segal, and S. Finkbeiner. 2004. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805-810.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 0023253287 scopus 로고
    • The distribution of vimentin and keratin in epithelial and nonepithelial neoplasms. A comprehensive immunohistochemical study on formalin- and alcohol-fixed tumors
    • Azumi, N., and H. Battifora. 1987. The distribution of vimentin and keratin in epithelial and nonepithelial neoplasms. A comprehensive immunohistochemical study on formalin- and alcohol-fixed tumors. Am. J. Clin. Pathol. 88:286-296.
    • (1987) Am. J. Clin. Pathol. , vol.88 , pp. 286-296
    • Azumi, N.1    Battifora, H.2
  • 7
    • 0021352916 scopus 로고
    • 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin
    • Blose, S. H., D. I. Meltzer, and J. R. Feramisco. 1984. 10-nm filaments are induced to collapse in living cells microinjected with monoclonal and polyclonal antibodies against tubulin. J. Cell Biol. 98:847-858.
    • (1984) J. Cell Biol. , vol.98 , pp. 847-858
    • Blose, S.H.1    Meltzer, D.I.2    Feramisco, J.R.3
  • 8
    • 0022497211 scopus 로고
    • Interaction of frog virus 3 with the cytomatrix. IV. Phosphorylation of vimentin precedes the reorganization of intermediate filaments around the virus assembly sites
    • Chen, M., R. Goorha, and K. G. Murti. 1986. Interaction of frog virus 3 with the cytomatrix. IV. Phosphorylation of vimentin precedes the reorganization of intermediate filaments around the virus assembly sites. J. Gen. Virol. 67:915-922.
    • (1986) J. Gen. Virol. , vol.67 , pp. 915-922
    • Chen, M.1    Goorha, R.2    Murti, K.G.3
  • 9
    • 0005175316 scopus 로고
    • Phosphorylation and disassembly of intermediate filaments in mitotic cells
    • Chou, Y. H., E. Rosevear, and R. D. Goldman. 1989. Phosphorylation and disassembly of intermediate filaments in mitotic cells. Proc. Natl. Acad. Sci. USA 86:1885-1889.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1885-1889
    • Chou, Y.H.1    Rosevear, E.2    Goldman, R.D.3
  • 10
    • 0025895855 scopus 로고
    • The regulation of intermediate filament reorganization in mitosis. P34cdc2 phosphorylates vimentin at a unique N-terminal site
    • Chou, Y. H., K. L. Ngai, and R. Goldman. 1991. The regulation of intermediate filament reorganization in mitosis. P34cdc2 phosphorylates vimentin at a unique N-terminal site. J. Biol. Chem. 266:7325-7328.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7325-7328
    • Chou, Y.H.1    Ngai, K.L.2    Goldman, R.3
  • 11
    • 0029861189 scopus 로고    scopus 로고
    • Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus
    • Cobbold, C., J. T. Whittle, and T. Wileman. 1996. Involvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virus. J. Virol. 70:8382-8390.
    • (1996) J. Virol. , vol.70 , pp. 8382-8390
    • Cobbold, C.1    Whittle, J.T.2    Wileman, T.3
  • 12
    • 0020328231 scopus 로고
    • An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells
    • Evans, R. M., and L. M. Fink. 1982. An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells. Cell 29:43-52.
    • (1982) Cell , vol.29 , pp. 43-52
    • Evans, R.M.1    Fink, L.M.2
  • 13
    • 0023009566 scopus 로고
    • Effects of colcemid and taxol on microtubules and intermediate filaments in chick embryo fibroblasts
    • Forryschaudies, S., J. M. Murray, Y. Toyama, and H. Holtzer. 1986. Effects of colcemid and taxol on microtubules and intermediate filaments in chick embryo fibroblasts. Cell Motil. Cytoskeleton 6:324-338.
    • (1986) Cell Motil. Cytoskeleton , vol.6 , pp. 324-338
    • Forryschaudies, S.1    Murray, J.M.2    Toyama, Y.3    Holtzer, H.4
  • 14
    • 84985759585 scopus 로고
    • Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments
    • Franke, W. W., C. Grand, C. Kuhn, B. W. Jackson, and K. Illmensee. 1982. Formation of cytoskeletal elements during mouse embryogenesis. III. Primary mesenchymal cells and the first appearance of vimentin filaments. Differentiation 23:43-59.
    • (1982) Differentiation , vol.23 , pp. 43-59
    • Franke, W.W.1    Grand, C.2    Kuhn, C.3    Jackson, B.W.4    Illmensee, K.5
  • 15
    • 0021133349 scopus 로고
    • Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal-antibody
    • Franke, W. W., C. Grund, C. Kuhn, V. P. Lehto, and I. Virtanen. 1984. Transient change of organization of vimentin filaments during mitosis as demonstrated by a monoclonal-antibody. Exp. Cell Res. 154:567-580.
    • (1984) Exp. Cell Res. , vol.154 , pp. 567-580
    • Franke, W.W.1    Grund, C.2    Kuhn, C.3    Lehto, V.P.4    Virtanen, I.5
  • 16
    • 0018733376 scopus 로고
    • Widespread occurrence of intermediate-sized filaments of the vimentin-type in cultured cells from diverse vertebrates
    • Franke, W. W., E. Schmid, S. Winter, M. Osborn, and K. Weber. 1979. Widespread occurrence of intermediate-sized filaments of the vimentin-type in cultured cells from diverse vertebrates. Exp. Cell Res. 123:25-46.
    • (1979) Exp. Cell Res. , vol.123 , pp. 25-46
    • Franke, W.W.1    Schmid, E.2    Winter, S.3    Osborn, M.4    Weber, K.5
  • 17
    • 0032496146 scopus 로고    scopus 로고
    • Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis
    • Goto, H., H. Kosako, K. Tanabe, M. Yanagida, M. Sakurai, M. Amano, K. Kaibuchi, and M. Inagaki. 1998. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J. Biol. Chem. 273:11728-11736.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11728-11736
    • Goto, H.1    Kosako, H.2    Tanabe, K.3    Yanagida, M.4    Sakurai, M.5    Amano, M.6    Kaibuchi, K.7    Inagaki, M.8
  • 18
    • 0025743437 scopus 로고
    • Coalignment of vimentin intermediate filaments with microtubules depends on kinesin
    • Gyoeva, F. K., and V. I. Gelfand. 1991. Coalignment of vimentin intermediate filaments with microtubules depends on kinesin. Nature 353:445-448.
    • (1991) Nature , vol.353 , pp. 445-448
    • Gyoeva, F.K.1    Gelfand, V.I.2
  • 19
    • 0035972239 scopus 로고    scopus 로고
    • Aggresomes resemble sites specialized for virus assembly
    • Heath, C. M., M. Windsor, and T. Wileman. 2001. Aggresomes resemble sites specialized for virus assembly. J. Cell Biol. 153:449-455.
    • (2001) J. Cell Biol. , vol.153 , pp. 449-455
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 20
    • 0037301422 scopus 로고    scopus 로고
    • Membrane association facilitates the correct processing of pp220 during production of the major matrix proteins of African swine fever virus
    • Heath, C. M., M. Windsor, and T. Wileman. 2003. Membrane association facilitates the correct processing of pp220 during production of the major matrix proteins of African swine fever virus. J. Virol. 77:1682-1690.
    • (2003) J. Virol. , vol.77 , pp. 1682-1690
    • Heath, C.M.1    Windsor, M.2    Wileman, T.3
  • 21
    • 0037182581 scopus 로고    scopus 로고
    • A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization
    • Helfand, B. T., A. Mikami, R. B. Vallee, and R. D. Goldman. 2002. A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization. J. Cell Biol. 157:795-806.
    • (2002) J. Cell Biol. , vol.157 , pp. 795-806
    • Helfand, B.T.1    Mikami, A.2    Vallee, R.B.3    Goldman, R.D.4
  • 22
    • 0035997377 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function
    • 2+/calmodulin- dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu. Rev. Biochem. 71:473-510.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 24
    • 0023239962 scopus 로고
    • Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
    • Inagaki, M., Y. Nishi, K. Nishizawa, M. Matsuyama, and C. Sato. 1987. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 328:649-652.
    • (1987) Nature , vol.328 , pp. 649-652
    • Inagaki, M.1    Nishi, Y.2    Nishizawa, K.3    Matsuyama, M.4    Sato, C.5
  • 25
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston, J. A., C. L. Ward, and R. R. Kopito. 1998. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 143:1883-1898.
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 26
    • 0025847755 scopus 로고
    • Calcium calmodulin-dependent protein-kinase mediates a pathway for transcriptional regulation
    • Kapiloff, M. S., J. M. Mathis, C. A. Nelson, C. R. Lin, and M. G. Rosenfeld. 1991. Calcium calmodulin-dependent protein-kinase mediates a pathway for transcriptional regulation. Proc. Natl. Acad. Sci. USA 88:3710-3714.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3710-3714
    • Kapiloff, M.S.1    Mathis, J.M.2    Nelson, C.A.3    Lin, C.R.4    Rosenfeld, M.G.5
  • 27
    • 0026806551 scopus 로고
    • African swine fever virus-induced DNA polymerase is resistant to aphidicolin
    • Marques, M. I., and J. V. Costa. 1992. African swine fever virus-induced DNA polymerase is resistant to aphidicolin. Virology 191:498-501.
    • (1992) Virology , vol.191 , pp. 498-501
    • Marques, M.I.1    Costa, J.V.2
  • 29
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer, T., P. I. Hanson, L. Stryer, and H. Schulman. 1992. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science 256:1199-1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 30
    • 0020618279 scopus 로고
    • Interaction of frog virus-3 with the cytoskeleton. I. Altered organization of microtubules, intermediate filaments, and microfilaments
    • Murti, K. G., and R. Goorha. 1983. Interaction of frog virus-3 with the cytoskeleton. I. Altered organization of microtubules, intermediate filaments, and microfilaments. J. Cell Biol. 96:1248-1257.
    • (1983) J. Cell Biol. , vol.96 , pp. 1248-1257
    • Murti, K.G.1    Goorha, R.2
  • 32
    • 1842614341 scopus 로고    scopus 로고
    • The subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs
    • Netherton, C., I. Rouiller, and T. Wileman. 2004. The subcellular distribution of multigene family 110 proteins of African swine fever virus is determined by differences in C-terminal KDEL endoplasmic reticulum retention motifs. J. Virol. 78:3710-3721.
    • (2004) J. Virol. , vol.78 , pp. 3710-3721
    • Netherton, C.1    Rouiller, I.2    Wileman, T.3
  • 33
    • 14544300928 scopus 로고    scopus 로고
    • Virus factories: Associations of cell organelles for viral replication and morphogenesis
    • Nova, R. R., G. Calderita, R. Arranz, J. Fontana, H. Granzow, and C. Risco. 2005. Virus factories: associations of cell organelles for viral replication and morphogenesis. Biol. Cell 97:147-172.
    • (2005) Biol. Cell , vol.97 , pp. 147-172
    • Nova, R.R.1    Calderita, G.2    Arranz, R.3    Fontana, J.4    Granzow, H.5    Risco, C.6
  • 35
    • 0032487522 scopus 로고    scopus 로고
    • Rapid movements of vimentin on microtubule tracks: Kinesin-dependent assembly of intermediate filament networks
    • Prahlad, V., M. Yoon, R. D. Moir, R. D. Vale, and R. D. Goldman. 1998. Rapid movements of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks. J. Cell Biol. 143:159-370.
    • (1998) J. Cell Biol. , vol.143 , pp. 159-370
    • Prahlad, V.1    Yoon, M.2    Moir, R.D.3    Vale, R.D.4    Goldman, R.D.5
  • 36
    • 0036149942 scopus 로고    scopus 로고
    • Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly
    • Risco, C., J. R. Rodriguez, C. Lopez-Iglesias, J. L. Carrascosa, M. Esteban, and D. Rodriguez. 2002. Endoplasmic reticulum-Golgi intermediate compartment membranes and vimentin filaments participate in vaccinia virus assembly. J. Virol. 76:1839-1855.
    • (2002) J. Virol. , vol.76 , pp. 1839-1855
    • Risco, C.1    Rodriguez, J.R.2    Lopez-Iglesias, C.3    Carrascosa, J.L.4    Esteban, M.5    Rodriguez, D.6
  • 37
    • 0025608671 scopus 로고
    • Dynamic properties of intermediate filaments: Disassembly and reassembly during mitosis in baby hamster kidney cells
    • Rosevear, E. R., M. McReynolds, and R. D. Goldman. 1990. Dynamic properties of intermediate filaments: disassembly and reassembly during mitosis in baby hamster kidney cells. Cell Motil. Cytoskeleton 17:150-166.
    • (1990) Cell Motil. Cytoskeleton , vol.17 , pp. 150-166
    • Rosevear, E.R.1    McReynolds, M.2    Goldman, R.D.3
  • 38
    • 0031937630 scopus 로고    scopus 로고
    • African swine fever virus is wrapped by the endoplasmic reticulum
    • Rouiller, I., S. M. Brookes, A. D. Hyatt, M. Windsor, and T. Wileman. 1998. African swine fever virus is wrapped by the endoplasmic reticulum. J. Virol. 72:2373-2387.
    • (1998) J. Virol. , vol.72 , pp. 2373-2387
    • Rouiller, I.1    Brookes, S.M.2    Hyatt, A.D.3    Windsor, M.4    Wileman, T.5
  • 39
    • 0027364732 scopus 로고
    • Identification of the gene encoding the major capsid protein of fish lymphocystis disease virus
    • Schnitzler, P., and G. Darai. 1993. Identification of the gene encoding the major capsid protein of fish lymphocystis disease virus. J. Gen. Virol. 74:2143-2150.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2143-2150
    • Schnitzler, P.1    Darai, G.2
  • 40
    • 0019991332 scopus 로고
    • The interaction of mammalian reoviruses with the cytoskeleton of monkey kidney Cv-1 cells
    • Sharpe, A. H., L. B. Chen, and B. N. Fields. 1982. The interaction of mammalian reoviruses with the cytoskeleton of monkey kidney Cv-1 cells. Virology 120:399-411.
    • (1982) Virology , vol.120 , pp. 399-411
    • Sharpe, A.H.1    Chen, L.B.2    Fields, B.N.3
  • 41
    • 0037064590 scopus 로고    scopus 로고
    • Unchain my heart, baby let me go - The entry and intracellular transport of HIV
    • Sodeik, B. 2002. Unchain my heart, baby let me go-the entry and intracellular transport of HIV. J. Cell Biol. 159:393-395.
    • (2002) J. Cell Biol. , vol.159 , pp. 393-395
    • Sodeik, B.1
  • 42
    • 0015817357 scopus 로고
    • The structure of icosahedral cytoplasmic deoxyriboviruses. II. An alternative model
    • Stoltz, A. B. 1973. The structure of icosahedral cytoplasmic deoxyriboviruses. II. An alternative model. J. Ultrastruct. Res. 43:58-74.
    • (1973) J. Ultrastruct. Res. , vol.43 , pp. 58-74
    • Stoltz, A.B.1
  • 43
    • 0029871758 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes
    • Takai, Y., M. Ogawara, Y. Tomono, C. Moritoh, S. Imajoh-Ohmi, O. Tsutsumi, Y. Taketani, and M. Inagaki. 1996. Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganization of intracellular membranes. J. Cell Biol. 133:141-149.
    • (1996) J. Cell Biol. , vol.133 , pp. 141-149
    • Takai, Y.1    Ogawara, M.2    Tomono, Y.3    Moritoh, C.4    Imajoh-Ohmi, S.5    Tsutsumi, O.6    Taketani, Y.7    Inagaki, M.8
  • 44
  • 47
    • 0028151022 scopus 로고
    • Visualization and function of vimentin phosphorylation by Cdc2 kinase during mitosis
    • Tsujimura, K., M. Ogawara, Y. Takeuchi, S. Imajohohmi, M. H. Ha, and M. Inagaki. 1994. Visualization and function of vimentin phosphorylation by Cdc2 kinase during mitosis. J. Biol. Chem. 269:31097-31106.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31097-31106
    • Tsujimura, K.1    Ogawara, M.2    Takeuchi, Y.3    Imajohohmi, S.4    Ha, M.H.5    Inagaki, M.6
  • 48
    • 0034796296 scopus 로고    scopus 로고
    • African swine fever virus infection of porcine aortic endothelial cells leads to inhibition of inflammatory responses, activation of the thrombotic state, and apoptosis
    • Vallee, I., S. W. G. Tait, and P. P. Powell. 2001. African swine fever virus infection of porcine aortic endothelial cells leads to inhibition of inflammatory responses, activation of the thrombotic state, and apoptosis. J. Virol. 75:10372-10382.
    • (2001) J. Virol. , vol.75 , pp. 10372-10382
    • Vallee, I.1    Tait, S.W.G.2    Powell, P.P.3
  • 49
    • 0018569549 scopus 로고
    • Macromolecular synthesis in cells infected by frog virus 3. XI. A ts mutant of frog virus 3 that is defective in late transcription
    • Willis, D. B., R. Goorha, and A. Granoff. 1979. Macromolecular synthesis in cells infected by frog virus 3. XI. A ts mutant of frog virus 3 that is defective in late transcription. Virology 98:328-335.
    • (1979) Virology , vol.98 , pp. 328-335
    • Willis, D.B.1    Goorha, R.2    Granoff, A.3
  • 50
    • 0032487443 scopus 로고    scopus 로고
    • Motile properties of vimentin intermediate filament networks in living cells
    • Yoon, M., R. D. Moir, V. Prahlad, and R. D. Goldman. 1998. Motile properties of vimentin intermediate filament networks in living cells. J. Cell Biol. 143:147-157.
    • (1998) J. Cell Biol. , vol.143 , pp. 147-157
    • Yoon, M.1    Moir, R.D.2    Prahlad, V.3    Goldman, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.