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Volumn 349, Issue 2, 2006, Pages 430-439

Phosphorylation of the HTLV-1 matrix L-domain-containing protein by virus-associated ERK-2 kinase

Author keywords

Budding; ERK 2; HTLV 1; L domain; Phosphorylation

Indexed keywords

ALANINE; AMINO ACID DERIVATIVE; MATRIX PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; VIRUS PROTEIN;

EID: 33646858158     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2006.02.043     Document Type: Article
Times cited : (12)

References (43)
  • 1
    • 3042694692 scopus 로고    scopus 로고
    • Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding
    • Blot V., Perugi F., Gay B., Prevost M.C., Briant L., Tangy F., Abriel H., Staub O., Dokhelar M.C., and Pique C. Nedd4.1-mediated ubiquitination and subsequent recruitment of Tsg101 ensure HTLV-1 Gag trafficking towards the multivesicular body pathway prior to virus budding. J. Cell Sci. 117 (2004) 2357-2367
    • (2004) J. Cell Sci. , vol.117 , pp. 2357-2367
    • Blot, V.1    Perugi, F.2    Gay, B.3    Prevost, M.C.4    Briant, L.5    Tangy, F.6    Abriel, H.7    Staub, O.8    Dokhelar, M.C.9    Pique, C.10
  • 2
    • 0242331750 scopus 로고    scopus 로고
    • PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]
    • Bouamr F., Melillo J.A., Wang M.Q., Nagashima K., de Los Santos M., Rein A., and Goff S.P. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]. J. Virol. 77 22 (2003) 11882-11895
    • (2003) J. Virol. , vol.77 , Issue.22 , pp. 11882-11895
    • Bouamr, F.1    Melillo, J.A.2    Wang, M.Q.3    Nagashima, K.4    de Los Santos, M.5    Rein, A.6    Goff, S.P.7
  • 3
    • 0021675931 scopus 로고
    • Polypeptides of Mason-Pfizer monkey virus: I. Synthesis and processing of the gag-gene products
    • Bradac J., and Hunter E. Polypeptides of Mason-Pfizer monkey virus: I. Synthesis and processing of the gag-gene products. Virology 138 2 (1984) 260-275
    • (1984) Virology , vol.138 , Issue.2 , pp. 260-275
    • Bradac, J.1    Hunter, E.2
  • 5
    • 0042317020 scopus 로고    scopus 로고
    • Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein
    • Cartier C., Hemonnot B., Gay B., Bardy M., Sanchiz C., Devaux C., and Briant L. Active cAMP-dependent protein kinase incorporated within highly purified HIV-1 particles is required for viral infectivity and interacts with viral capsid protein. J. Biol. Chem. 278 37 (2003) 35211-35219
    • (2003) J. Biol. Chem. , vol.278 , Issue.37 , pp. 35211-35219
    • Cartier, C.1    Hemonnot, B.2    Gay, B.3    Bardy, M.4    Sanchiz, C.5    Devaux, C.6    Briant, L.7
  • 6
    • 0033050343 scopus 로고    scopus 로고
    • Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras
    • Craven R.C., Harty R.N., Paragas J., Palese P., and Wills J.W. Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J. Virol. 73 4 (1999) 3359-3365
    • (1999) J. Virol. , vol.73 , Issue.4 , pp. 3359-3365
    • Craven, R.C.1    Harty, R.N.2    Paragas, J.3    Palese, P.4    Wills, J.W.5
  • 7
    • 9744221135 scopus 로고    scopus 로고
    • Retrovirus budding
    • Demirov D.G., and Freed E.O. Retrovirus budding. Virus Res. 106 2 (2004) 87-102
    • (2004) Virus Res. , vol.106 , Issue.2 , pp. 87-102
    • Demirov, D.G.1    Freed, E.O.2
  • 8
    • 0028816439 scopus 로고
    • Virions released from cells transfected with a molecular clone of human T-cell leukemia virus type I give rise to primary and secondary infections of T cells
    • Derse D., Mikovits J., Polianova M., Felber B.K., and Ruscetti F. Virions released from cells transfected with a molecular clone of human T-cell leukemia virus type I give rise to primary and secondary infections of T cells. J. Virol. 69 3 (1995) 1907-1912
    • (1995) J. Virol. , vol.69 , Issue.3 , pp. 1907-1912
    • Derse, D.1    Mikovits, J.2    Polianova, M.3    Felber, B.K.4    Ruscetti, F.5
  • 9
    • 0032935035 scopus 로고    scopus 로고
    • Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions
    • Dettenhofer M., and Yu X.F. Highly purified human immunodeficiency virus type 1 reveals a virtual absence of Vif in virions. J. Virol. 73 2 (1999) 1460-1467
    • (1999) J. Virol. , vol.73 , Issue.2 , pp. 1460-1467
    • Dettenhofer, M.1    Yu, X.F.2
  • 10
    • 0031925435 scopus 로고    scopus 로고
    • Particle size determinants in the human immunodeficiency virus type 1 Gag protein
    • Garnier L., Ratner L., Rovinski B., Cao S.X., and Wills J.W. Particle size determinants in the human immunodeficiency virus type 1 Gag protein. J. Virol. 72 6 (1998) 4667-4677
    • (1998) J. Virol. , vol.72 , Issue.6 , pp. 4667-4677
    • Garnier, L.1    Ratner, L.2    Rovinski, B.3    Cao, S.X.4    Wills, J.W.5
  • 11
    • 3543025697 scopus 로고    scopus 로고
    • The host cell MAPKinase ERK2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1
    • Hémonnot B., Cartier C., Gay B., Rebuffat S., Bardy M., Devaux C., Boyer V., and Briant L. The host cell MAPKinase ERK2 regulates viral assembly and release by phosphorylating the p6gag protein of HIV-1. J. Biol. Chem. 279 31 (2004) 32426-32434
    • (2004) J. Biol. Chem. , vol.279 , Issue.31 , pp. 32426-32434
    • Hémonnot, B.1    Cartier, C.2    Gay, B.3    Rebuffat, S.4    Bardy, M.5    Devaux, C.6    Boyer, V.7    Briant, L.8
  • 12
    • 0022239332 scopus 로고
    • Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus
    • Henderson L.E., Sowder R., Smythers G., Benveniste R.E., and Oroszlan S. Purification and N-terminal amino acid sequence comparisons of structural proteins from retrovirus-D/Washington and Mason-Pfizer monkey virus. J. Virol. 55 3 (1985) 778-787
    • (1985) J. Virol. , vol.55 , Issue.3 , pp. 778-787
    • Henderson, L.E.1    Sowder, R.2    Smythers, G.3    Benveniste, R.E.4    Oroszlan, S.5
  • 13
    • 0033106369 scopus 로고    scopus 로고
    • Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels
    • Hicke L. Gettin' down with ubiquitin: turning off cell-surface receptors, transporters and channels. Trends Cell Biol. 9 3 (1999) 107-112
    • (1999) Trends Cell Biol. , vol.9 , Issue.3 , pp. 107-112
    • Hicke, L.1
  • 14
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M., Orenstein J.M., Martin M.A., and Freed E.O. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69 11 (1995) 6810-6818
    • (1995) J. Virol. , vol.69 , Issue.11 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 15
    • 0036308521 scopus 로고    scopus 로고
    • Virion-associated protein kinases
    • Hui E.K. Virion-associated protein kinases. Cell. Mol. Life Sci. 59 6 (2002) 920-931
    • (2002) Cell. Mol. Life Sci. , vol.59 , Issue.6 , pp. 920-931
    • Hui, E.K.1
  • 17
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells
    • Kikonyogo A., Bouamr F., Vana M.L., Xiang Y., Aiyar A., Carter C., and Leis J. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl. Acad. Sci. U.S.A. 98 20 (2001) 11199-11204
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.20 , pp. 11199-11204
    • Kikonyogo, A.1    Bouamr, F.2    Vana, M.L.3    Xiang, Y.4    Aiyar, A.5    Carter, C.6    Leis, J.7
  • 18
    • 0036776607 scopus 로고    scopus 로고
    • The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process
    • Le Blanc I., Prevost M.C., Dokhelar M.C., and Rosenberg A.R. The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process. J. Virol. 76 19 (2002) 10024-10029
    • (2002) J. Virol. , vol.76 , Issue.19 , pp. 10024-10029
    • Le Blanc, I.1    Prevost, M.C.2    Dokhelar, M.C.3    Rosenberg, A.R.4
  • 19
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu P.J., Zhou X.Z., Shen M., and Lu K.P. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283 5406 (1999) 1325-1328
    • (1999) Science , vol.283 , Issue.5406 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 20
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano J., Zang T., and Bieniasz P.D. Role of ESCRT-I in retroviral budding. J. Virol. 77 8 (2003) 4794-4804
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 21
    • 0034704145 scopus 로고    scopus 로고
    • The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Morris D.P., and Greenleaf A.L. The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 275 51 (2000) 39935-39943
    • (2000) J. Biol. Chem. , vol.275 , Issue.51 , pp. 39935-39943
    • Morris, D.P.1    Greenleaf, A.L.2
  • 22
    • 0033615705 scopus 로고    scopus 로고
    • Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-End formation
    • Morris D.P., Phatnani H.P., and Greenleaf A.L. Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3′-End formation. J. Biol. Chem. 274 44 (1999) 31583-31587
    • (1999) J. Biol. Chem. , vol.274 , Issue.44 , pp. 31583-31587
    • Morris, D.P.1    Phatnani, H.P.2    Greenleaf, A.L.3
  • 23
    • 0036145336 scopus 로고    scopus 로고
    • The Late-domain-containing protein p6 is the predominant phosphoprotein of human immunodeficiency virus type 1 particles
    • Muller B., Patschinsky T., and Krausslich H.G. The Late-domain-containing protein p6 is the predominant phosphoprotein of human immunodeficiency virus type 1 particles. J. Virol. 76 3 (2002) 1015-1024
    • (2002) J. Virol. , vol.76 , Issue.3 , pp. 1015-1024
    • Muller, B.1    Patschinsky, T.2    Krausslich, H.G.3
  • 24
    • 0018735115 scopus 로고
    • Characterization of 40,000- and 25,000-dalton intermediate precursors to Rauscher murine leukemia virus gag gene products
    • Naso R.B., Karshin W.L., Wu Y.H., and Arlinghaus R.B. Characterization of 40,000- and 25,000-dalton intermediate precursors to Rauscher murine leukemia virus gag gene products. J. Virol. 32 1 (1979) 187-198
    • (1979) J. Virol. , vol.32 , Issue.1 , pp. 187-198
    • Naso, R.B.1    Karshin, W.L.2    Wu, Y.H.3    Arlinghaus, R.B.4
  • 25
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott D.E., Coren L.V., Copeland T.D., Kane B.P., Johnson D.G., Sowder II R.C., Yoshinaka Y., Oroszlan S., Arthur L.O., and Henderson L.E. Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J. Virol. 72 4 (1998) 2962-2968
    • (1998) J. Virol. , vol.72 , Issue.4 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder II, R.C.6    Yoshinaka, Y.7    Oroszlan, S.8    Arthur, L.O.9    Henderson, L.E.10
  • 29
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A., Chau V., and Wills J.W. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. U.S.A. 97 24 (2000) 13069-13074
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.24 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 30
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer B.A., Parent L.J., Wills J.W., and Montelaro R.C. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71 9 (1997) 6541-6546
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 32
    • 0017296211 scopus 로고
    • Specific binding of the type C viral core protein p12 with purified viral RNA
    • Sen A., Sherr C.J., and Todaro G.J. Specific binding of the type C viral core protein p12 with purified viral RNA. Cell 7 1 (1976) 21-32
    • (1976) Cell , vol.7 , Issue.1 , pp. 21-32
    • Sen, A.1    Sherr, C.J.2    Todaro, G.J.3
  • 33
    • 0017337048 scopus 로고
    • Phosphorylation of murine type C viral p12 proteins regulates their extent of binding to the homologous viral RNA
    • Sen A., Sherr C.J., and Todaro G.J. Phosphorylation of murine type C viral p12 proteins regulates their extent of binding to the homologous viral RNA. Cell 10 3 (1977) 489-496
    • (1977) Cell , vol.10 , Issue.3 , pp. 489-496
    • Sen, A.1    Sherr, C.J.2    Todaro, G.J.3
  • 35
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B., Calistri A., Craig S., Popova E., and Gottlinger H.G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114 6 (2003) 689-699
    • (2003) Cell , vol.114 , Issue.6 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 36
    • 0034704216 scopus 로고    scopus 로고
    • New wrinkles for an old domain
    • Sudol M., and Hunter T. New wrinkles for an old domain. Cell 103 7 (2000) 1001-1004
    • (2000) Cell , vol.103 , Issue.7 , pp. 1001-1004
    • Sudol, M.1    Hunter, T.2
  • 37
    • 0033885803 scopus 로고    scopus 로고
    • Structural basis for phosphoserine-proline recognition by group IV WW domains
    • Verdecia M.A., Bowman M.E., Lu K.P., Hunter T., and Noel J.P. Structural basis for phosphoserine-proline recognition by group IV WW domains. Nat. Struct. Biol. 7 8 (2000) 639-643
    • (2000) Nat. Struct. Biol. , vol.7 , Issue.8 , pp. 639-643
    • Verdecia, M.A.1    Bowman, M.E.2    Lu, K.P.3    Hunter, T.4    Noel, J.P.5
  • 38
    • 0034700119 scopus 로고    scopus 로고
    • Ubiquitin in retrovirus assembly: actor or bystander?
    • Vogt V.M. Ubiquitin in retrovirus assembly: actor or bystander?. Proc. Natl. Acad. Sci. U.S.A. 97 24 (2000) 12945-12947
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.24 , pp. 12945-12947
    • Vogt, V.M.1
  • 39
    • 0347634395 scopus 로고    scopus 로고
    • Both the PPPY and PTAP motifs are involved in human T-cell leukemia virus type 1 particle release
    • Wang H., Machesky N.J., and Mansky L.M. Both the PPPY and PTAP motifs are involved in human T-cell leukemia virus type 1 particle release. J. Virol. 78 3 (2004) 1503-1512
    • (2004) J. Virol. , vol.78 , Issue.3 , pp. 1503-1512
    • Wang, H.1    Machesky, N.J.2    Mansky, L.M.3
  • 40
    • 0031968983 scopus 로고    scopus 로고
    • A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release
    • Yasuda J., and Hunter E. A proline-rich motif (PPPY) in the Gag polyprotein of Mason-Pfizer monkey virus plays a maturation-independent role in virion release. J. Virol. 72 5 (1998) 4095-4103
    • (1998) J. Virol. , vol.72 , Issue.5 , pp. 4095-4103
    • Yasuda, J.1    Hunter, E.2
  • 41
    • 0020062627 scopus 로고
    • In vitro phosphorylation of murine leukemia virus proteins: specific phosphorylation of Pr65gag, the precursor of the internal core antigens
    • Yoshinaka Y., and Luftig R.B. In vitro phosphorylation of murine leukemia virus proteins: specific phosphorylation of Pr65gag, the precursor of the internal core antigens. Virology 116 1 (1982) 181-195
    • (1982) Virology , vol.116 , Issue.1 , pp. 181-195
    • Yoshinaka, Y.1    Luftig, R.B.2
  • 42
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan B., Campbell S., Bacharach E., Rein A., and Goff S.P. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74 16 (2000) 7250-7260
    • (2000) J. Virol. , vol.74 , Issue.16 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 43
    • 0037302292 scopus 로고    scopus 로고
    • Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection
    • Yueh A., and Goff S.P. Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection. J. Virol. 77 3 (2003) 1820-1829
    • (2003) J. Virol. , vol.77 , Issue.3 , pp. 1820-1829
    • Yueh, A.1    Goff, S.P.2


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