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Volumn 244, Issue 2, 1998, Pages 343-351

Adenovirus death protein, a transmembrane protein encoded in the E3 region, is palmitoylated at the cytoplasmic tail

Author keywords

[No Author keywords available]

Indexed keywords

ADENOVIRUS; ARTICLE; HUMAN; HUMAN CELL; IMMUNE RESPONSE; PALMITOYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN PROCESSING; SITE DIRECTED MUTAGENESIS; THIN LAYER CHROMATOGRAPHY; VIRUS REPLICATION; VIRUS TRANSCRIPTION;

EID: 0032503232     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9135     Document Type: Article
Times cited : (24)

References (51)
  • 1
    • 0024384342 scopus 로고
    • Fatty acid acylation of the fusion glycoprotein of human respiratory syncytial virus
    • Arumugham R. G., Seid R. C., Doyle G., Hildreth S. W., Paradiso P. R. Fatty acid acylation of the fusion glycoprotein of human respiratory syncytial virus. J. Biol. Chem. 264:1989;10339-10342.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10339-10342
    • Arumugham, R.G.1    Seid, R.C.2    Doyle, G.3    Hildreth, S.W.4    Paradiso, P.R.5
  • 2
    • 0025602322 scopus 로고
    • Myelin proteolipid protein contains thioester-linked fatty acids
    • Bizzozero A., Good L. K. Myelin proteolipid protein contains thioester-linked fatty acids. J. Neurochem. 55:1990;1986-1992.
    • (1990) J. Neurochem. , vol.55 , pp. 1986-1992
    • Bizzozero, A.1    Good, L.K.2
  • 3
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoprotein takes place after exit from the endoplasmic reticulum
    • Bonatti S., Migliaccio G., Simons K. Palmitylation of viral membrane glycoprotein takes place after exit from the endoplasmic reticulum. J. Biol. Chem. 264:1989;12590-12595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 4
    • 0028234577 scopus 로고
    • N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization
    • Cadwallader K. A., Paterson H., MacDonald S. G., Hancock J. F. N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization. Mol. Cell. Biol. 14:1994;4722-4730.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4722-4730
    • Cadwallader, K.A.1    Paterson, H.2    MacDonald, S.G.3    Hancock, J.F.4
  • 5
    • 0029107952 scopus 로고
    • Modification of membrane permeability by animal viruses
    • Carrasco L. Modification of membrane permeability by animal viruses. Adv. Virus Res. 45:1995;61-112.
    • (1995) Adv. Virus Res. , vol.45 , pp. 61-112
    • Carrasco, L.1
  • 6
    • 0028351930 scopus 로고
    • Lipid modifications of G proteins
    • Casey P. J. Lipid modifications of G proteins. Curr. Opin. Cell. Biol. 6:1994;219-225.
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 219-225
    • Casey, P.J.1
  • 7
    • 0028935780 scopus 로고
    • Protein Lipidation in cell signaling
    • Casey P. J. Protein Lipidation in cell signaling. Science. 268:1995;221-225.
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 8
    • 0019446161 scopus 로고
    • Deletion mutants of adenovirus 2: Isolation and initial characterization of virus carrying mutations near the right end of the viral genome
    • Challberg S. S., Ketner G. Deletion mutants of adenovirus 2: Isolation and initial characterization of virus carrying mutations near the right end of the viral genome. Virology. 114:1981;196-209.
    • (1981) Virology , vol.114 , pp. 196-209
    • Challberg, S.S.1    Ketner, G.2
  • 9
    • 0026717615 scopus 로고
    • Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor
    • Crise B., Rose J. K. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. J. Biol. Chem. 267:1992;13593-13597.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13593-13597
    • Crise, B.1    Rose, J.K.2
  • 10
    • 0028020919 scopus 로고
    • The palmitoylated cysteine of the cytoplasmic tail of a 2A-adrenergic receptors confers subtype-specific agonist-promoted down-regulation
    • Eason M. G., Jacinto M. T., Theiss C. T., Liggett S. B. The palmitoylated cysteine of the cytoplasmic tail of a 2A-adrenergic receptors confers subtype-specific agonist-promoted down-regulation. Proc. Natl. Acad. Sci. 91:1994;11178-11182.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 11178-11182
    • Eason, M.G.1    Jacinto, M.T.2    Theiss, C.T.3    Liggett, S.B.4
  • 11
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst T. R., Niles E. G., Studier F. W., Moss B. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA. 83:1986;8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 13
    • 0025364097 scopus 로고
    • The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids
    • Gaedigk-Nitschko K., Schlesinger M. J. The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids. Virology. 175:1990;274-281.
    • (1990) Virology , vol.175 , pp. 274-281
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 14
    • 0025373966 scopus 로고
    • Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure
    • Gaedigk-Nitschko K., Ding M., Aach Levy M., Schlesinger M. J. Site-directed mutations in the Sindbis virus 6K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure. Virology. 175:1990;282-291.
    • (1990) Virology , vol.175 , pp. 282-291
    • Gaedigk-Nitschko, K.1    Ding, M.2    Aach Levy, M.3    Schlesinger, M.J.4
  • 15
    • 0029112711 scopus 로고
    • Localization of th epalmitoylation site in the transmembrane protein p12E of Friend murine leukaemia virus
    • Hensel J., Hintz M., Karas M., Linder D., Stahl B., Geyer R. Localization of th epalmitoylation site in the transmembrane protein p12E of Friend murine leukaemia virus. Eur. J. Biochem. 232:1995;373-380.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 373-380
    • Hensel, J.1    Hintz, M.2    Karas, M.3    Linder, D.4    Stahl, B.5    Geyer, R.6
  • 16
    • 0027419559 scopus 로고
    • Site-directed mutations in the sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding
    • Ivanova L., Schlesinger M. J. Site-directed mutations in the sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding. J. Virol. 67:1993;2546-2551.
    • (1993) J. Virol. , vol.67 , pp. 2546-2551
    • Ivanova, L.1    Schlesinger, M.J.2
  • 17
    • 0030026752 scopus 로고    scopus 로고
    • Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
    • Jin H., Subbarao K., Bagai S., Leser G. P., Murphy B. R., Lamb R. A. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70:1996;1406-1414.
    • (1996) J. Virol. , vol.70 , pp. 1406-1414
    • Jin, H.1    Subbarao, K.2    Bagai, S.3    Leser, G.P.4    Murphy, B.R.5    Lamb, R.A.6
  • 19
    • 0023276003 scopus 로고
    • Acylation of the 176R (19-kilodalton) early region 1B protein of human adenovirus type 5
    • McGlade C. J., Tremblay M. L., Yee S.-P., Ross R., Branton P. E. Acylation of the 176R (19-kilodalton) early region 1B protein of human adenovirus type 5. J. Virol. 61:1987;3227-3234.
    • (1987) J. Virol. , vol.61 , pp. 3227-3234
    • McGlade, C.J.1    Tremblay, M.L.2    Yee, S.-P.3    Ross, R.4    Branton, P.E.5
  • 20
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G., Parenti M., Magee A. I. The dynamic role of palmitoylation in signal transduction. TIBS. 20:1995;181-186.
    • (1995) TIBS , vol.20 , pp. 181-186
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 22
    • 0028911202 scopus 로고
    • Receptor regulation of G protein palmitoylation
    • Mumby S. M., Muntz K. H. Receptor regulation of G protein palmitoylation. Biochem. Soc. Trans. 23:1995;156-160.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 156-160
    • Mumby, S.M.1    Muntz, K.H.2
  • 23
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve C. W., Williams D. Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9:1990;3857-3866.
    • (1990) EMBO J. , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 24
    • 0029033820 scopus 로고
    • Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment
    • Philipp H. C., Schroth B. C., Veit M., Krumbiegel M., Herrmann A., Schmidt M. F. Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment. Virology. 210:1995;20-28.
    • (1995) Virology , vol.210 , pp. 20-28
    • Philipp, H.C.1    Schroth, B.C.2    Veit, M.3    Krumbiegel, M.4    Herrmann, A.5    Schmidt, M.F.6
  • 25
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto L. H., Holsinger L. J., Lamb R. A. Influenza virus M2 protein has ion channel activity. Cell. 69:1992;517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 26
    • 0029134534 scopus 로고
    • Acylation of viral glycoproteins: Structural requirements for pamitoylation of transmembrane proteins
    • Ponimaskin E., Schmidt M. F. G. Acylation of viral glycoproteins: Structural requirements for pamitoylation of transmembrane proteins. Biochem. Soc. Trans. 23:1995;565-568.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 565-568
    • Ponimaskin, E.1    Schmidt, M.F.G.2
  • 27
    • 0029793327 scopus 로고    scopus 로고
    • Differential fatty acid selection during biosynthetic S-acylation of a transmembrane protein (HEF) and other proteins in insect cells (Sf9) and in mammalian cells (CV1)
    • Reverey H., Veit M., Ponimaskin E., Schmidt M. F. G. Differential fatty acid selection during biosynthetic S-acylation of a transmembrane protein (HEF) and other proteins in insect cells (Sf9) and in mammalian cells (CV1). J. Biol. Chem. 271:1996;23607-23610.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23607-23610
    • Reverey, H.1    Veit, M.2    Ponimaskin, E.3    Schmidt, M.F.G.4
  • 28
    • 0027064711 scopus 로고
    • The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane
    • Scaria A., Tollefson A. E., Saha S. K., Wold W. S. M. The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane. Virology. 191:1992;743-753.
    • (1992) Virology , vol.191 , pp. 743-753
    • Scaria, A.1    Tollefson, A.E.2    Saha, S.K.3    Wold, W.S.M.4
  • 29
    • 0019171287 scopus 로고
    • Fatty acid acylation of proteins in cultured cells
    • Schlesinger M. J., Magee A. I., Schmidt M. F. G. Fatty acid acylation of proteins in cultured cells. J. Biol. Chem. 256:1980;10021-10024.
    • (1980) J. Biol. Chem. , vol.256 , pp. 10021-10024
    • Schlesinger, M.J.1    Magee, A.I.2    Schmidt, M.F.G.3
  • 30
    • 0024263339 scopus 로고
    • Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1)
    • Schmidt M., Schmidt M. F. G., Rott R. Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki Forest virus E1). J. Biol. Chem. 263:1988;18635-18639.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18635-18639
    • Schmidt, M.1    Schmidt, M.F.G.2    Rott, R.3
  • 31
    • 0024346820 scopus 로고
    • Fatty acylation of proteins
    • Schmidt M. F. G. Fatty acylation of proteins. Biochim. Biophys. Acta. 988:1989;411-426.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 411-426
    • Schmidt, M.F.G.1
  • 32
    • 0019332459 scopus 로고
    • Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins
    • Schmidt M. F. G., Schlesinger M. J. Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins. J. Biol. Chem. 255:1980;3334-3339.
    • (1980) J. Biol. Chem. , vol.255 , pp. 3334-3339
    • Schmidt, M.F.G.1    Schlesinger, M.J.2
  • 33
    • 0018643375 scopus 로고
    • Fatty acid binding to vesicular stomatitis virus glycoprotein - A new type of posttranslational modification of the viral glycoprotein
    • Schmidt M. F. G., Schlesinger M. J. Fatty acid binding to vesicular stomatitis virus glycoprotein - a new type of posttranslational modification of the viral glycoprotein. Cell. 17:1979;813-819.
    • (1979) Cell , vol.17 , pp. 813-819
    • Schmidt, M.F.G.1    Schlesinger, M.J.2
  • 34
    • 0018459056 scopus 로고
    • Evidence for covalent attachment of fatty acids to sindbis virus glycoproteins
    • Schmidt M. F. G., Bracha M., Schlesinger M. J. Evidence for covalent attachment of fatty acids to sindbis virus glycoproteins. Proc. Natl. Acad. Sci. USA. 81:1979;1687-1691.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1687-1691
    • Schmidt, M.F.G.1    Bracha, M.2    Schlesinger, M.J.3
  • 35
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;596-572.
    • (1997) Nature , vol.387 , pp. 596-572
    • Simons, K.1    Ikonen, E.2
  • 36
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens J. E., Roth M. G., Matlin K. S. Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell. Biol. 108:1989;821-832.
    • (1989) J. Cell. Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 39
    • 0030003101 scopus 로고    scopus 로고
    • The E3-11.6kDa adenovirus death protein (ADP) is required for efficient cell death: Characterization of cells infected with ADP mutants
    • Tollefson A. E., Ryerse J. S., Scaria A., Hermiston T. W., Wold W. S. M. The E3-11.6kDa adenovirus death protein (ADP) is required for efficient cell death: Characterization of cells infected with ADP mutants. Virology. 220:1996b;152-162.
    • (1996) Virology , vol.220 , pp. 152-162
    • Tollefson, A.E.1    Ryerse, J.S.2    Scaria, A.3    Hermiston, T.W.4    Wold, W.S.M.5
  • 40
    • 0029872241 scopus 로고    scopus 로고
    • The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells
    • Tollefson A. E., Scaria A., Hermiston T. W., Ryerse J. S., Wold L. J., Wold W. S. M. The adenovirus death protein (E3-11.6K) is required at very late stages of infection for efficient cell lysis and release of adenovirus from infected cells. J. Virol. 70:1996a;2296-2306.
    • (1996) J. Virol. , vol.70 , pp. 2296-2306
    • Tollefson, A.E.1    Scaria, A.2    Hermiston, T.W.3    Ryerse, J.S.4    Wold, L.J.5    Wold, W.S.M.6
  • 41
    • 0026610807 scopus 로고
    • The 11,600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection
    • Tollefson A. E., Scaria A., Saha S. K., Wold W. S. M. The 11,600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection. J. Virol. 66:1992;3633-3642.
    • (1992) J. Virol. , vol.66 , pp. 3633-3642
    • Tollefson, A.E.1    Scaria, A.2    Saha, S.K.3    Wold, W.S.M.4
  • 42
    • 0027137047 scopus 로고
    • Timing of palmitoylation of influenza virus hemagglutinin
    • Veit M., Schmidt M. F. G. Timing of palmitoylation of influenza virus hemagglutinin. FEBS Lett. 336:1993;243-247.
    • (1993) FEBS Lett. , vol.336 , pp. 243-247
    • Veit, M.1    Schmidt, M.F.G.2
  • 43
    • 0025754428 scopus 로고
    • The M2 protein of influenza A virus is acylated
    • Veit M., Klenk H.-D., Kendal A. P., Rott R. The M2 protein of influenza A virus is acylated. J. Gen. Virol. 72:1991a;1461-1465.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1461-1465
    • Veit, M.1    Klenk, H.-D.2    Kendal, A.P.3    Rott, R.4
  • 44
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit M., Kretzschmar E., Kuroda K., Garten W., Schmid M. F. G., Klenk H.-D., Rott R. Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65:1991b;2491-2500.
    • (1991) J. Virol. , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmid, M.F.G.5    Klenk, H.-D.6    Rott, R.7
  • 45
    • 0029833443 scopus 로고    scopus 로고
    • Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins
    • Veit M., Reverey H., Schmidt M. F. G. Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins. Biochem. J. 318:1996;163-172.
    • (1996) Biochem. J. , vol.318 , pp. 163-172
    • Veit, M.1    Reverey, H.2    Schmidt, M.F.G.3
  • 46
    • 0023831579 scopus 로고
    • An adenovirus mRNA which encodes a 14,700-Mr protein that maps to the last open reading frame in region E3 is expressed during infection
    • Wang E. W., Scott M. O., Ricciardi R. P. An adenovirus mRNA which encodes a 14,700-Mr protein that maps to the last open reading frame in region E3 is expressed during infection. J. Virol. 62:1988;1456-1459.
    • (1988) J. Virol. , vol.62 , pp. 1456-1459
    • Wang, E.W.1    Scott, M.O.2    Ricciardi, R.P.3
  • 47
    • 0021706440 scopus 로고
    • Nuclear envelope localization of an adenovirus tumor antigen maintains the integrity of cellular DNA
    • White E., Blose S. H., Stillman B. W. Nuclear envelope localization of an adenovirus tumor antigen maintains the integrity of cellular DNA. Mol. Cell. Biol. 4:1984;2865-2875.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2865-2875
    • White, E.1    Blose, S.H.2    Stillman, B.W.3
  • 49
    • 0030198535 scopus 로고    scopus 로고
    • Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits
    • Yang C., Compans R. W. Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits. Virology. 221:1996;87-97.
    • (1996) Virology , vol.221 , pp. 87-97
    • Yang, C.1    Compans, R.W.2
  • 50
    • 0028784818 scopus 로고
    • The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated
    • Yang C., Spies C. P., Compans R. W. The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated. Proc. Natl. Acad. Sci. USA. 92:1995;9871-9875.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9871-9875
    • Yang, C.1    Spies, C.P.2    Compans, R.W.3
  • 51
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation
    • Zurcher T., Luo G., Palese P. Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68:1994;5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zurcher, T.1    Luo, G.2    Palese, P.3


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