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Volumn 73, Issue 11, 1999, Pages 8975-8981

Palmitoylation of the intracytoplasmic R peptide of the transmembrane envelope protein in Moloney murine leukemia virus

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 0032853026     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.11.8975-8981.1999     Document Type: Article
Times cited : (25)

References (49)
  • 1
    • 0017225203 scopus 로고
    • Two-dimensional gel electrophoresis of membrane proteins
    • Ames, G. F.-L., and K. Nikaido. 1976. Two-dimensional gel electrophoresis of membrane proteins. Biochemistry 15:616-623.
    • (1976) Biochemistry , vol.15 , pp. 616-623
    • Ames, G.F.-L.1    Nikaido, K.2
  • 2
    • 0020694132 scopus 로고
    • Entry of murine retrovirus into mouse fibroblasts
    • Andersen, K. B., and B. A. Nexø. 1983. Entry of murine retrovirus into mouse fibroblasts. Virology 125:85-98.
    • (1983) Virology , vol.125 , pp. 85-98
    • Andersen, K.B.1    Nexø, B.A.2
  • 3
    • 0026608630 scopus 로고
    • Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses
    • Battini, J.-L., J. M. Heard, and O. Danos. 1992. Receptor choice determinants in the envelope glycoproteins of amphotropic, xenotropic, and polytropic murine leukemia viruses. J. Virol. 66:1468-1475.
    • (1992) J. Virol. , vol.66 , pp. 1468-1475
    • Battini, J.-L.1    Heard, J.M.2    Danos, O.3
  • 4
    • 0021955901 scopus 로고
    • Protein fatty acyltransferase is located in the rough endoplasmic reticulum
    • Berger, M., and M. F. G. Schmidt. 1985. Protein fatty acyltransferase is located in the rough endoplasmic reticulum. FEBS Lett. 187:289-294.
    • (1985) FEBS Lett. , vol.187 , pp. 289-294
    • Berger, M.1    Schmidt, M.F.G.2
  • 5
    • 0024322074 scopus 로고
    • Palmitoylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum
    • Bonatti, S., G. Migliaccio, and K. Simons. 1989. Palmitoylation of viral membrane glycoproteins takes place after exit from the endoplasmic reticulum. J. Biol. Chem. 264:12590-12595.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 6
    • 0028234577 scopus 로고
    • N-terminally myristoylated ras proteins require palmitoylation or a polybasic domain for plasma membrane localization
    • Cadwallader, K. A., H. Paterson, S. G. Macdonald, and J. F. Hancock. 1994. N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization. Mol. Cell. Biol. 14:4722-4730.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4722-4730
    • Cadwallader, K.A.1    Paterson, H.2    Macdonald, S.G.3    Hancock, J.F.4
  • 7
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey, P. J. 1995. Protein lipidation in cell signaling. Science 268:221-224.
    • (1995) Science , vol.268 , pp. 221-224
    • Casey, P.J.1
  • 8
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain, J. P. 1979. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 9
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 å resolution
    • Pass, D., S. C. Harrison, and P. S. Kim. 1996. Retrovirus envelope domain at 1.7 Å resolution. Nat. Struct. Biol. 3:465-469.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 465-469
    • Pass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 10
    • 0020364597 scopus 로고
    • Evidence for a glycoprotein "signal" involved in transport between subcellular organelles. Two membrane glycoproteins encoded by murine leukemia virus reach the cell surface at different rates
    • Fitting, T., and D. Kabat, 1982. Evidence for a glycoprotein "signal" involved in transport between subcellular organelles. Two membrane glycoproteins encoded by murine leukemia virus reach the cell surface at different rates. J. Biol. Chem. 257:14011-14017.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14011-14017
    • Fitting, T.1    Kabat, D.2
  • 11
    • 0021591109 scopus 로고
    • Rous sarcoma virus p19 and gp35 can be chemically crosslinked to high molecular weight complexes
    • Gebhardt, A., J. V. Bosch, A. Ziemiecki, and R. R. Friis. 1984. Rous sarcoma virus p19 and gp35 can be chemically crosslinked to high molecular weight complexes. J. Mol. Biol. 174:297-317.
    • (1984) J. Mol. Biol. , vol.174 , pp. 297-317
    • Gebhardt, A.1    Bosch, J.V.2    Ziemiecki, A.3    Friis, R.R.4
  • 12
    • 0019844429 scopus 로고
    • Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope protein involves removal of a COOH-terminal peptide
    • Green, N., T. M. Shinnick, O. Witte, A. Ponticelli, J. G. Suteliffe, and R. A. Lerner. 1981. Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope protein involves removal of a COOH-terminal peptide. Proc. Natl. Acad. Sci. USA 78:6023-6027.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6023-6027
    • Green, N.1    Shinnick, T.M.2    Witte, O.3    Ponticelli, A.4    Suteliffe, J.G.5    Lerner, R.A.6
  • 13
    • 0032503232 scopus 로고    scopus 로고
    • Adenovirus death protein, a transmembrane protein encoded in the E3 region, is palmitoylated at the cytoplasmic tail
    • Hausmann, J., D. Ortmann, E. Witt, M. Veit, and W. Seidel. 1998. Adenovirus death protein, a transmembrane protein encoded in the E3 region, is palmitoylated at the cytoplasmic tail. Virology 244:343-351.
    • (1998) Virology , vol.244 , pp. 343-351
    • Hausmann, J.1    Ortmann, D.2    Witt, E.3    Veit, M.4    Seidel, W.5
  • 14
    • 0021690345 scopus 로고
    • Quantitative separation of murine leukemia virus protein by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products
    • Henderson, L. E., R. Sowder, T. D. Copeland, G. Smythers, and S. Oroszlan. 1984. Quantitative separation of murine leukemia virus protein by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products. J. Virol. 52:492-500.
    • (1984) J. Virol. , vol.52 , pp. 492-500
    • Henderson, L.E.1    Sowder, R.2    Copeland, T.D.3    Smythers, G.4    Oroszlan, S.5
  • 15
    • 0029112711 scopus 로고
    • Localization of the palmitoylation site in the transmembrane protein p12E of friend murine leukemia virus
    • Hensel, J., M. Hintz, M. Karas, D. Linder, B. Stahl, and R. Geyer. 1995. Localization of the palmitoylation site in the transmembrane protein p12E of Friend murine leukemia virus. Eur. J. Biochem. 232:373-380.
    • (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
  • 18
    • 0027419559 scopus 로고
    • Site-directed mutations in the sindbis virus e2 glycoprotein identify palmitoylation sites and affect virus budding
    • Ivanova, L., and M. J. Schlesinger. 1993. Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding. J. Virol. 67:2546-2551.
    • (1993) J. Virol. , vol.67 , pp. 2546-2551
    • Ivanova, L.1    Schlesinger, M.J.2
  • 19
    • 0030991945 scopus 로고    scopus 로고
    • Two distinct oncornaviruses harbor an intracytoplasmic tyrosine-based basolateral targeting signal in their viral envelope glycoprotein
    • Lodge, R., L. Delamarre, J.-P. Lalonde, J. Alvarado, D. A. Sanders, M.-C. Ookhélar, E. A. Cohen, and G. Lemay. 1997. Two distinct oncornaviruses harbor an intracytoplasmic tyrosine-based basolateral targeting signal in their viral envelope glycoprotein. J. Virol. 71:5696-5702.
    • (1997) J. Virol. , vol.71 , pp. 5696-5702
    • Lodge, R.1    Delamarre, L.2    Lalonde, J.-P.3    Alvarado, J.4    Sanders, D.A.5    Ookhélar, M.-C.6    Cohen, E.A.7    Lemay, G.8
  • 20
    • 0020597763 scopus 로고
    • A simple and rapid method for the preparation of plasma membranes
    • Maeda, T., K. Balakrishnan, and S. Q. Mehdi. 1983. A simple and rapid method for the preparation of plasma membranes. Biochim. Biophys. Acta 731:115-120.
    • (1983) Biochim. Biophys. Acta , vol.731 , pp. 115-120
    • Maeda, T.1    Balakrishnan, K.2    Mehdi, S.Q.3
  • 21
    • 0023276003 scopus 로고
    • Acylation of the 176R (19-kilodalton) early region IB protein of human adenovirus type 5
    • McGlade, C. J., M. L. Tremblay, S.-P. Yee, R. Ross, and P. E. Branton. 1987. Acylation of the 176R (19-kilodalton) early region IB protein of human adenovirus type 5. J. Virol. 61:3227-3234.
    • (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
  • 22
    • 0023547909 scopus 로고
    • Protein binding of palmitate measured by transmembrane diffusion through polyethylene
    • Moran, J. B., F. J. Burczynski, R. F. Cheek, T. Bopp, and E. L. Forker. 1987. Protein binding of palmitate measured by transmembrane diffusion through polyethylene. Anal. Biochem. 167:394-399.
    • (1987) Anal. Biochem. , vol.167 , pp. 394-399
    • Moran, J.B.1    Burczynski, F.J.2    Cheek, R.F.3    Bopp, T.4    Forker, E.L.5
  • 23
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby, S. M. 1997. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9:148-154.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 24
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C. W., and D. Williams. 1990. Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9:3857-3866.
    • (1990) EMBO J. , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 25
    • 0344324433 scopus 로고
    • Nitrocellulose membranes as solid phase in immunoblotting
    • O. J. Bjerrum and N. H. H. Heegaard (ed.), CRC Press, Inc., Boca Raton, Fla.
    • Nyholm, L., and J. Ramlau. 1988. Nitrocellulose membranes as solid phase in immunoblotting, p. 101-108. In O. J. Bjerrum and N. H. H. Heegaard (ed.), Handbook of immunoblotting of proteins, vol. 1. CRC Press, Inc., Boca Raton, Fla.
    • (1988) Handbook of Immunoblotting of Proteins , vol.1 , pp. 101-108
    • Nyholm, L.1    Ramlau, J.2
  • 26
    • 0016711037 scopus 로고
    • High-resolution two-dimensional electrophoresis of proteins
    • O'Farrell, P. H. 1975. High-resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 27
    • 0029033820 scopus 로고
    • Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment
    • Philipp, H. C., B. Schroth, M. Veit, M. Krumbiegel, A. Herrmann, and M. F. G. Schmidt. 1995. Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment. Virology 210:20-28.
    • (1995) Virology , vol.210 , pp. 20-28
    • Philipp, H.C.1    Schroth, B.2    Veit, M.3    Krumbiegel, M.4    Herrmann, A.5    Schmidt, M.F.G.6
  • 28
    • 0028271720 scopus 로고
    • pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: Implications for the role of the R peptide and p12E TM in viral entry
    • Ragheb, J. A., and W. F. Anderson. 1994. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry. J. Virol. 68:3220-3231.
    • (1994) J. Virol. , vol.68 , pp. 3220-3231
    • Ragheb, J.A.1    Anderson, W.F.2
  • 29
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of a retroviral transmembrane protein: P15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus env protein
    • Rein, A., J. Mirro, J. G. Haynes, S. M. Ernst, and K. Nagashima. 1994. Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein. J. Virol. 68:1773-1781.
    • (1994) J. Virol. , vol.68 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 30
    • 0028173679 scopus 로고
    • Myristylation and palmitoylation of src family members: The fats of the matter
    • Resh, M. D. 1994. Myristylation and palmitoylation of Src family members: the fats of the matter. Cell 76:411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 31
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh, M. D. 1996. Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins. Cell. Signal. 8:403-412.
    • (1996) Cell. Signal. , vol.8 , pp. 403-412
    • Resh, M.D.1
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 33
    • 0344324432 scopus 로고    scopus 로고
    • M.S. thesis. Royal Danish School of Pharmacy, Copenhagen, Denmark
    • Schmidt, G., and S. Willemann. 1998. M.S. thesis. Royal Danish School of Pharmacy, Copenhagen, Denmark.
    • (1998)
    • Schmidt, G.1    Willemann, S.2
  • 34
    • 0021513714 scopus 로고
    • The transfer of myristic and other fatty acids on lipid and viral protein acceptors in cultured cells infected with Semliki forest virus and influenza virus
    • Schmidt, M. F. G. 1984. The transfer of myristic and other fatty acids on lipid and viral protein acceptors in cultured cells infected with Semliki forest virus and influenza virus. EMBO J. 3:2295-2300.
    • (1984) EMBO J. , vol.3 , pp. 2295-2300
    • Schmidt, M.F.G.1
  • 35
    • 0024263339 scopus 로고
    • Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki forest virus E1)
    • Schmidt, M., M. F. G. Schmidt, and R. Rott. 1988. Chemical identification of cysteine as palmitoylation site in a transmembrane protein (Semliki forest virus E1). J. Biol. Chem. 263:18635-18639.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18635-18639
    • Schmidt, M.1    Schmidt, M.F.G.2    Rott, R.3
  • 36
    • 0024346820 scopus 로고
    • Fatty acylation of proteins
    • Schmidt, M. F. G. 1989. Fatty acylation of proteins. Biochim. Biophys. Acta 988:411-426.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 411-426
    • Schmidt, M.F.G.1
  • 37
    • 0021806159 scopus 로고
    • Maturation of murine leukemia virus Env proteins in the absence of other viral proteins
    • Schultz, A., and A. Rein. 1985. Maturation of murine leukemia virus Env proteins in the absence of other viral proteins. Virology 145:335-339.
    • (1985) Virology , vol.145 , pp. 335-339
    • Schultz, A.1    Rein, A.2
  • 38
    • 0023188263 scopus 로고
    • The covalent modification of eukaryotic proteins with lipid
    • Sefton, B. M., and J. E. Buss. 1987. The covalent modification of eukaryotic proteins with lipid. J. Cell Biol. 104:1449-1453.
    • (1987) J. Cell Biol. , vol.104 , pp. 1449-1453
    • Sefton, B.M.1    Buss, J.E.2
  • 39
    • 0021075713 scopus 로고
    • Membrane association and defective transport of spleen focus-forming virus glycoproteins
    • Srinivas, R. V., and R. W. Compans. 1983. Membrane association and defective transport of spleen focus-forming virus glycoproteins. J. Biol. Chem. 258:14718-14724.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14718-14724
    • Srinivas, R.V.1    Compans, R.W.2
  • 40
    • 0031732763 scopus 로고    scopus 로고
    • Palmitoylation of human thyrotropin receptor: Slower intracellular trafficking of the palmitoylation-defective mutant
    • Tanaka, K., Y. Nagayama, E. Nishihara, H. Namba, S. Yamashita, and M. Niwa. 1998. Palmitoylation of human thyrotropin receptor: slower intracellular trafficking of the palmitoylation-defective mutant. Endocrinology 139: 803-806.
    • (1998) Endocrinology , vol.139 , pp. 803-806
    • Tanaka, K.1    Nagayama, Y.2    Nishihara, E.3    Namba, H.4    Yamashita, S.5    Niwa, M.6
  • 42
    • 0024490871 scopus 로고
    • Different palmitoylation of paramyxovirus glycoproteins
    • Veit, M., F. G. Schmidt, and R. Rott. 1989. Different palmitoylation of paramyxovirus glycoproteins. Virology 168:173-176.
    • (1989) Virology , vol.168 , pp. 173-176
    • Veit, M.1    Schmidt, F.G.2    Rott, R.3
  • 43
    • 0027137047 scopus 로고
    • Timing of palmitoylation of influenza virus hemagglutinin
    • Veit, M., and M. F. G. Schmidt. 1993. Timing of palmitoylation of influenza virus hemagglutinin. FEBS Lett. 336:243-247.
    • (1993) FEBS Lett. , vol.336 , pp. 243-247
    • Veit, M.1    Schmidt, M.F.G.2
  • 44
    • 0029833443 scopus 로고    scopus 로고
    • Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins
    • Veit, M., H. Reverey, and M. F. G. Schmidt. 1996. Cytoplasmic tail length influences fatty acid selection for acylation of viral glycoproteins. Biochem. J. 318:163-172.
    • (1996) Biochem. J. , vol.318 , pp. 163-172
    • Veit, M.1    Reverey, H.2    Schmidt, M.F.G.3
  • 45
    • 0031616556 scopus 로고    scopus 로고
    • Membrane targeting via protein palmitoylation
    • Veit, M., and M. F. G. Schmidt. 1998. Membrane targeting via protein palmitoylation. Methods Mol. Biol. 88:227-239.
    • (1998) Methods Mol. Biol. , vol.88 , pp. 227-239
    • Veit, M.1    Schmidt, M.F.G.2
  • 46
    • 0018390929 scopus 로고
    • Structure of the murine leukemia virus envelope glycoprotein precursor
    • Witte, O. N., and D. F. Wirth. 1979. Structure of the murine leukemia virus envelope glycoprotein precursor. J. Virol. 29:735-743.
    • (1979) J. Virol. , vol.29 , pp. 735-743
    • Witte, O.N.1    Wirth, D.F.2
  • 47
    • 0028784818 scopus 로고
    • The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated
    • Yang, C., C. P. Spies, and R. W. Compans. 1995. The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated. Proc. Natl. Acad. Sci. USA 92:9871-9875.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9871-9875
    • Yang, C.1    Spies, C.P.2    Compans, R.W.3
  • 48
    • 0029656198 scopus 로고    scopus 로고
    • Analysis of the cell fusion activities of chimeric simian immunodeficiency virus-murine leukemia virus envelope proteins: Inhibitory effects of the R-peptide
    • Yang, C., and R. W. Compans. 1996. Analysis of the cell fusion activities of chimeric simian immunodeficiency virus-murine leukemia virus envelope proteins: inhibitory effects of the R-peptide. J. Virol. 70:248-254.
    • (1996) J. Virol. , vol.70 , pp. 248-254
    • Yang, C.1    Compans, R.W.2
  • 49
    • 0030198535 scopus 로고    scopus 로고
    • Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits
    • Yang, C., and R. W. Compans. 1996. Palmitoylation of the murine leukemia virus envelope glycoprotein transmembrane subunits. Virology 221:87-97.
    • (1996) Virology , vol.221 , pp. 87-97
    • Yang, C.1    Compans, R.W.2


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