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Volumn 84, Issue 9, 2010, Pages 4158-4171

Venezuelan equine encephalitis virus capsid protein forms a tetrameric complex with CRM1 and importin α/β that obstructs nuclear pore complex function

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CAPSID PROTEIN; CELL NUCLEUS RECEPTOR; EXPORTIN 1; KARYOPHERIN ALPHA; KARYOPHERIN BETA; NUCLEOPORIN; PEPTIDE; TETRAMER;

EID: 77950854511     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02554-09     Document Type: Article
Times cited : (94)

References (51)
  • 1
    • 43249104024 scopus 로고    scopus 로고
    • Structural and nonstructural protein genome regions of eastern equine encephalitis virus are determinants of interferon sensitivity and murine virulence
    • Aguilar, P. V., A. P. Adams, E. Wang, W. Kang, A. S. Carrara, M. Anishchenko, I. Frolov, and S. C. Weaver. 2008. Structural and nonstructural protein genome regions of eastern equine encephalitis virus are determinants of interferon sensitivity and murine virulence. J. Virol. 82:4920-4930.
    • (2008) J. Virol. , vol.82 , pp. 4920-4930
    • Aguilar, P.V.1    Adams, A.P.2    Wang, E.3    Kang, W.4    Carrara, A.S.5    Anishchenko, M.6    Frolov, I.7    Weaver, S.C.8
  • 5
    • 41949140033 scopus 로고    scopus 로고
    • Venezuelan equine encephalitis virus capsid protein inhibits nuclear import in mammalian but not in mosquito cells
    • DOI 10.1128/JVI.02330-07
    • Atasheva, S., N. Garmashova, I. Frolov, and E. Frolova. 2008. Venezuelan equine encephalitis virus capsid protein inhibits nuclear import in mammalian but not in mosquito cells. J. Virol. 82:4028-4041. (Pubitemid 351521238)
    • (2008) Journal of Virology , vol.82 , Issue.8 , pp. 4028-4041
    • Atasheva, S.1    Garmashova, N.2    Frolov, I.3    Frolova, E.4
  • 6
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • DOI 10.1126/science.1104808
    • Beck, M., F. Forster, M. Ecke, J. M. Plitzko, F. Melchior, G. Gerisch, W. Baumeister, and O. Medalia. 2004. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306:1387-1390. (Pubitemid 39532518)
    • (2004) Science , vol.306 , Issue.5700 , pp. 1387-1390
    • Beck, M.1    Forster, F.2    Ecke, M.3    Plitzko, J.M.4    Melchior, F.5    Gerisch, G.6    Baumeister, W.7    Medalia, O.8
  • 7
    • 0037452599 scopus 로고    scopus 로고
    • The strategy for coupling the RanGTP gradient to nuclear protein export
    • Becskei, A., and I. W. Mattaj. 2003. The strategy for coupling the RanGTP gradient to nuclear protein export. Proc. Natl. Acad. Sci. U. S. A. 100:1717-1722.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1717-1722
    • Becskei, A.1    Mattaj, I.W.2
  • 8
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • DOI 10.1083/jcb.152.2.411
    • Ben-Efraim, I., and L. Gerace. 2001. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J. Cell Biol. 152:411-417. (Pubitemid 34285609)
    • (2001) Journal of Cell Biology , vol.152 , Issue.2 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 11
    • 0036146229 scopus 로고    scopus 로고
    • Positively charged amino acid substitutions in the e2 envelope glycoprotein are associated with the emergence of Venezuelan equine encephalitis virus
    • Brault, A. C., A. M. Powers, E. C. Holmes, C. H. Woelk, and S. C. Weaver. 2002. Positively charged amino acid substitutions in the e2 envelope glycoprotein are associated with the emergence of Venezuelan equine encephalitis virus. J. Virol. 76:1718-1730.
    • (2002) J. Virol. , vol.76 , pp. 1718-1730
    • Brault, A.C.1    Powers, A.M.2    Holmes, E.C.3    Woelk, C.H.4    Weaver, S.C.5
  • 13
    • 5044235320 scopus 로고    scopus 로고
    • Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358
    • DOI 10.1038/sj.emboj.7600370
    • Engelsma, D., R. Bernad, J. Calafat, and M. Fornerod. 2004. Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358. EMBO J. 23:3643-3652. (Pubitemid 39336286)
    • (2004) EMBO Journal , vol.23 , Issue.18 , pp. 3643-3652
    • Engelsma, D.1    Bernad, R.2    Calafat, J.3    Fornerod, M.4
  • 14
    • 48749107741 scopus 로고    scopus 로고
    • A supraphysiological nuclear export signal is required for parvovirus nuclear export
    • Engelsma, D., N. Valle, A. Fish, N. Salome, J. M. Almendral, and M. Fornerod. 2008. A supraphysiological nuclear export signal is required for parvovirus nuclear export. Mol. Biol. Cell 19:2544-2552.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2544-2552
    • Engelsma, D.1    Valle, N.2    Fish, A.3    Salome, N.4    Almendral, J.M.5    Fornerod, M.6
  • 16
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • DOI 10.1016/S0092-8674(00)80371-2
    • Fornerod, M., M. Ohno, M. Yoshida, and I. W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90:1051-1060. (Pubitemid 27408519)
    • (1997) Cell , vol.90 , Issue.6 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 17
    • 34547679515 scopus 로고    scopus 로고
    • A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes
    • DOI 10.1016/j.cell.2007.06.024, PII S009286740700791X
    • Frey, S., and D. Gorlich. 2007. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130:512-523. (Pubitemid 47208521)
    • (2007) Cell , vol.130 , Issue.3 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 18
    • 0030941093 scopus 로고    scopus 로고
    • Sindbis virus replicons and sindbis virus: Assembly of chimeras and of particles deficient in virus RNA
    • Frolov, I., E. Frolova, and S. Schlesinger. 1997. Sindbis virus replicons and Sindbis virus: assembly of chimeras and of particles deficient in virus RNA. J. Virol. 71:2819-2829. (Pubitemid 27119921)
    • (1997) Journal of Virology , vol.71 , Issue.4 , pp. 2819-2829
    • Frolov, I.1    Frolova, E.2    Schlesinger, S.3
  • 19
    • 37049005174 scopus 로고    scopus 로고
    • Analysis of Venezuelan equine encephalitis virus capsid protein function in the inhibition of cellular transcription
    • DOI 10.1128/JVI.01576-07
    • Garmashova, N., S. Atasheva, W. Kang, S. C. Weaver, E. Frolova, and I. Frolov. 2007. Analysis of Venezuelan equine encephalitis virus capsid protein function in the inhibition of cellular transcription. J. Virol. 81:13552-13565. (Pubitemid 350247849)
    • (2007) Journal of Virology , vol.81 , Issue.24 , pp. 13552-13565
    • Garmashova, N.1    Atasheva, S.2    Kang, W.3    Weaver, S.C.4    Frolova, E.5    Frolov, I.6
  • 20
    • 33744937066 scopus 로고    scopus 로고
    • Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription
    • DOI 10.1128/JVI.02739-05
    • Garmashova, N., R. Gorchakov, E. Frolova, and I. Frolov. 2006. Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription. J. Virol. 80:5686-5696. (Pubitemid 43849146)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5686-5696
    • Garmashova, N.1    Gorchakov, R.2    Frolova, E.3    Frolov, I.4
  • 21
    • 33847199327 scopus 로고    scopus 로고
    • The old world and new world alphaviruses use different virus-specific proteins for induction of transcriptional shutoff
    • DOI 10.1128/JVI.02073-06
    • Garmashova, N., R. Gorchakov, E. Volkova, S. Paessler, E. Frolova, and I. Frolov. 2007. The Old World and New World alphaviruses use different virus-specific proteins for induction of transcriptional shutoff. J. Virol. 81:2472-2484. (Pubitemid 46303363)
    • (2007) Journal of Virology , vol.81 , Issue.5 , pp. 2472-2484
    • Garmashova, N.1    Gorchakov, R.2    Volkova, E.3    Paessler, S.4    Frolova, E.5    Frolov, I.6
  • 23
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • DOI 10.1093/emboj/cdg113
    • Gorlich, D., M. J. Seewald, and K. Ribbeck. 2003. Characterization of Randriven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J. 22:1088-1100. (Pubitemid 36313593)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1088-1100
    • Gorlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 24
    • 0000804266 scopus 로고
    • Alphavirus pathogenesis and immunity
    • S. Schlesinger and M. J. Schlesinger (ed.), Plenum Press, New York, NY
    • Griffin, D. 1986. Alphavirus pathogenesis and immunity, p. 209-250. In S. Schlesinger and M. J. Schlesinger (ed.), The Togaviridae and Flaviviridae. Plenum Press, New York, NY.
    • (1986) The Togaviridae and Flaviviridae , pp. 209-250
    • Griffin, D.1
  • 25
    • 0142091706 scopus 로고    scopus 로고
    • Inhibition of nucleo-cytoplasmic trafficking by RNA viruses: Targeting the nuclear pore complex
    • Gustin, K. E. 2003. Inhibition of nucleo-cytoplasmic trafficking by RNA viruses: targeting the nuclear pore complex. Virus Res. 95:35-44.
    • (2003) Virus Res. , vol.95 , pp. 35-44
    • Gustin, K.E.1
  • 26
    • 0034630158 scopus 로고    scopus 로고
    • A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals
    • Henderson, B. R., and A. Eleftheriou. 2000. A comparison of the activity, sequence specificity, and CRM1-dependence of different nuclear export signals. Exp. Cell Res. 256:213-224.
    • (2000) Exp. Cell Res. , vol.256 , pp. 213-224
    • Henderson, B.R.1    Eleftheriou, A.2
  • 27
    • 0030810744 scopus 로고    scopus 로고
    • Inhibition of Ran guanosine triphosphatase-dependent nuclear transport by the matrix protein of vesicular stomatitis virus
    • Her, L. S., E. Lund, and J. E. Dahlberg. 1997. Inhibition of Ran guanosine triphosphatase-dependent nuclear transport by the matrix protein of vesicular stomatitis virus. Science 276:1845-1848.
    • (1997) Science , vol.276 , pp. 1845-1848
    • Her, L.S.1    Lund, E.2    Dahlberg, J.E.3
  • 28
    • 33748509106 scopus 로고    scopus 로고
    • Alphavirus capsid protein helix I controls a checkpoint in nucleocapsid core assembly
    • Hong, E. M., R. Perera, and R. J. Kuhn. 2006. Alphavirus capsid protein helix I controls a checkpoint in nucleocapsid core assembly. J. Virol. 80:8848-8855.
    • (2006) J. Virol. , vol.80 , pp. 8848-8855
    • Hong, E.M.1    Perera, R.2    Kuhn, R.J.3
  • 29
    • 0016168739 scopus 로고
    • Correlates to increased lethality of attenuated Venezuelan encephalitis virus vaccine for immunosuppressed hamsters
    • Jahrling, P. B., E. Dendy, and G. A. Eddy. 1974. Correlates to increased lethality of attenuated Venezuelan encephalitis virus vaccine for immunosuppressed hamsters. Infect. Immun. 9:924-930.
    • (1974) Infect. Immun. , vol.9 , pp. 924-930
    • Jahrling, P.B.1    Dendy, E.2    Eddy, G.A.3
  • 30
    • 0000113157 scopus 로고    scopus 로고
    • Alphaviruses
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), 3rd ed. Lippincott-Raven, New York, NY
    • Johnston, R. E., and C. J. Peters. 1996. Alphaviruses, p. 843-898. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven, New York, NY.
    • (1996) Fields Virology , pp. 843-898
    • Johnston, R.E.1    Peters, C.J.2
  • 31
    • 48749104048 scopus 로고    scopus 로고
    • Innate immune modulation by RNA viruses: Emerging insights from functional genomics
    • Katze, M. G., J. L. Fornek, R. E. Palermo, K. A. Walters, and M. J. Korth. 2008. Innate immune modulation by RNA viruses: emerging insights from functional genomics. Nat. Rev. Immunol. 8:644-654.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 644-654
    • Katze, M.G.1    Fornek, J.L.2    Palermo, R.E.3    Walters, K.A.4    Korth, M.J.5
  • 32
    • 0033577860 scopus 로고    scopus 로고
    • A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export
    • Kehlenbach, R. H., A. Dickmanns, A. Kehlenbach, T. Guan, and L. Gerace. 1999. A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell Biol. 145:645-657.
    • (1999) J. Cell Biol. , vol.145 , pp. 645-657
    • Kehlenbach, R.H.1    Dickmanns, A.2    Kehlenbach, A.3    Guan, T.4    Gerace, L.5
  • 35
    • 65249084031 scopus 로고    scopus 로고
    • Reengineering ribosome export
    • Lo, K. Y., and A. W. Johnson. 2009. Reengineering ribosome export. Mol. Biol. Cell 20:1545-1554.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1545-1554
    • Lo, K.Y.1    Johnson, A.W.2
  • 36
    • 0030775693 scopus 로고    scopus 로고
    • Nuclear import of U snRNPs requires importin beta
    • Palacios, I., M. Hetzer, S. A. Adam, and I. W. Mattaj. 1997. Nuclear import of U snRNPs requires importin beta. EMBO J. 16:6783-6792. (Pubitemid 27503490)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6783-6792
    • Palacios, I.1    Hetzer, M.2    Adam, S.A.3    Mattaj, L.W.4
  • 37
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel, S. S., B. J. Belmont, J. M. Sante, and M. F. Rexach. 2007. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129:83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 40
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • DOI 10.1093/emboj/21.11.2664
    • Ribbeck, K., and D. Gorlich. 2002. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21:2664-2671. (Pubitemid 34619382)
    • (2002) EMBO Journal , vol.21 , Issue.11 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 42
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., J. D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B. T. Chait. 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635-651.
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 43
    • 0001059961 scopus 로고
    • The Venezuelan equine encephalomyelitis complex of group A arthropod-borne viruses, including Mucambo and Pixuna from the Amazon region of Brazil
    • Shope, R. E., O. R. Causey, and A. H. De Andrade. 1964. The Venezuelan equine encephalomyelitis complex of group A arthropod-borne viruses, including Mucambo and Pixuna from the Amazon region of Brazil. Am. J. Trop. Med. Hyg. 13:723-727.
    • (1964) Am. J. Trop. Med. Hyg. , vol.13 , pp. 723-727
    • Shope, R.E.1    Causey, O.R.2    De Andrade, A.H.3
  • 44
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss, J. H., and E. G. Strauss. 1994. The alphaviruses: gene expression, replication, and evolution. Microbiol. Rev. 58:491-562.
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 45
    • 0033995285 scopus 로고    scopus 로고
    • Nucleic acid-dependent cross-linking of the nucleocapsid protein of Sindbis virus
    • DOI 10.1128/JVI.74.9.4302-4309.2000
    • Tellinghuisen, T. L., and R. J. Kuhn. 2000. Nucleic acid-dependent crosslinking of the nucleocapsid protein of Sindbis virus. J. Virol. 74:4302-4309. (Pubitemid 30214438)
    • (2000) Journal of Virology , vol.74 , Issue.9 , pp. 4302-4309
    • Tellinghuisen, T.L.1    Kuhn, R.J.2
  • 46
    • 30044437341 scopus 로고    scopus 로고
    • The efficient packaging of Venezuelan equine encephalitis virus-specific RNAs into viral particles is determined by nsP1-3 synthesis
    • DOI 10.1016/j.virol.2005.09.010, PII S0042682205005714
    • Volkova, E., R. Gorchakov, and I. Frolov. 2006. The efficient packaging of Venezuelan equine encephalitis virus-specific RNAs into viral particles is determined by nsP1-3 synthesis. Virology 344:315-327. (Pubitemid 43049620)
    • (2006) Virology , vol.344 , Issue.2 , pp. 315-327
    • Volkova, E.1    Gorchakov, R.2    Frolov, I.3
  • 48
    • 42449146575 scopus 로고    scopus 로고
    • Role of sindbis virus capsid protein region II in nucleocapsid core assembly and encapsidation of genomic RNA
    • DOI 10.1128/JVI.01936-07
    • Warrier, R., B. R. Linger, B. L. Golden, and R. J. Kuhn. 2008. Role of Sindbis virus capsid protein region II in nucleocapsid core assembly and encapsidation of genomic RNA. J. Virol. 82:4461-4470. (Pubitemid 351563682)
    • (2008) Journal of Virology , vol.82 , Issue.9 , pp. 4461-4470
    • Warrier, R.1    Linger, B.R.2    Golden, B.L.3    Kuhn, R.J.4
  • 50
    • 0028988731 scopus 로고
    • Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences
    • Weis, K., I. W. Mattaj, and A. I. Lamond. 1995. Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science 268:1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 51
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., J. L. Meinkoth, R. Y. Tsien, and S. S. Taylor. 1995. Identification of a signal for rapid export of proteins from the nucleus. Cell 82:463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4


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