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Volumn 146, Issue 1, 1999, Pages 113-124

Intracellular localization of proteasomal degradation of a viral antigen

Author keywords

Antigen presentation; Molecular chaperone; Nuclear proteins proteolysis; Proteasome; Ubiquitin immunology

Indexed keywords

PROTEASOME; VIRUS ANTIGEN; VIRUS NUCLEOPROTEIN;

EID: 0033549496     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.146.1.113     Document Type: Article
Times cited : (194)

References (38)
  • 1
    • 0032524940 scopus 로고    scopus 로고
    • Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides
    • Antón, L.C., H.L. Snyder, J.R. Bennink, A. Vinitsky, M. Orlowski, A. Porgador, and J.W. Yewdell. 1998. Dissociation of proteasomal degradation of biosynthesized viral proteins from generation of MHC class I-associated antigenic peptides. J. Immunol. 160:4859-4868.
    • (1998) J. Immunol. , vol.160 , pp. 4859-4868
    • Antón, L.C.1    Snyder, H.L.2    Bennink, J.R.3    Vinitsky, A.4    Orlowski, M.5    Porgador, A.6    Yewdell, J.W.7
  • 3
    • 0030850669 scopus 로고    scopus 로고
    • Proteasome inhibitors and antigen presentation
    • Bogyo, M., M. Gaczynska, and H.L. Ploegh. 1997. Proteasome inhibitors and antigen presentation. Biopolymers. 43:269-280.
    • (1997) Biopolymers. , vol.43 , pp. 269-280
    • Bogyo, M.1    Gaczynska, M.2    Ploegh, H.L.3
  • 4
    • 0022402441 scopus 로고
    • Vaccinia virus expression vector: Coexpression of β-galactosidase provides visual screening of recombinant virus plaques
    • Chakrabarti, S., K. Brechling, and B. Moss. 1985. Vaccinia virus expression vector: coexpression of β-galactosidase provides visual screening of recombinant virus plaques. Mol. Cell. Biol. 5:3403-3409.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3403-3409
    • Chakrabarti, S.1    Brechling, K.2    Moss, B.3
  • 5
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover, A. 1998. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO (Eur. Mol. Biol. Organ.) J. 17:7151-7160.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 6
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings, C.J., M.A. Mancini, B. Antalffy, D.B. DeFranco. H.T. Orr, and H.Y. Zoghbi. 1998. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19:148-154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 8
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • Desterro, J.M., M.S. Rodriguez, and R.T. Hay. 1998. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol. Cell. 2:233-239.
    • (1998) Mol. Cell. , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 9
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck, J.A., G.G. Maul, W.H.J. Miller, J.D. Chen, A. Kakizuka, and R.M. Evans. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell. 76:333-343.
    • (1994) Cell. , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller, W.H.J.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 10
    • 0031878851 scopus 로고    scopus 로고
    • The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
    • Everett, R.D., P. Freemont, H. Saitoh, M. Dasso, A. Orr, M. Kathoria, and J. Parkinson. 1998. The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms. J. Virol. 72:6581-6591.
    • (1998) J. Virol. , vol.72 , pp. 6581-6591
    • Everett, R.D.1    Freemont, P.2    Saitoh, H.3    Dasso, M.4    Orr, A.5    Kathoria, M.6    Parkinson, J.7
  • 11
    • 0032889557 scopus 로고    scopus 로고
    • The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication
    • Everett, R.D., M. Meredith, and A. Orr. 1999. The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication. J. Virol. 73:417-426.
    • (1999) J. Virol. , vol.73 , pp. 417-426
    • Everett, R.D.1    Meredith, M.2    Orr, A.3
  • 12
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimuro, M., H. Sadada, and H. Yokosawa. 1994. Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett. 349:173-180.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sadada, H.2    Yokosawa, H.3
  • 13
    • 0028894198 scopus 로고
    • Human proteasome analysed with monoclonal antibodies
    • Hendil, K.B., P. Kristensen, and W. Uerkvitz. 1995. Human proteasome analysed with monoclonal antibodies. Biochem. J. 305:245-252.
    • (1995) Biochem. J. , vol.305 , pp. 245-252
    • Hendil, K.B.1    Kristensen, P.2    Uerkvitz, W.3
  • 14
    • 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
  • 16
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D.H., and A.L. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 17
    • 0342871691 scopus 로고    scopus 로고
    • Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: Effects on replication, transcription, translation, and the cellular stress response
    • Mimnaugh, E.G., H.Y. Chen, J.R. Davie, J.E. Celis, and L. Neckers. 1997. Rapid deubiquitination of nucleosomal histones in human tumor cells caused by proteasome inhibitors and stress response inducers: effects on replication, transcription, translation, and the cellular stress response. Biochemistry. 36:14418-14429.
    • (1997) Biochemistry , vol.36 , pp. 14418-14429
    • Mimnaugh, E.G.1    Chen, H.Y.2    Davie, J.R.3    Celis, J.E.4    Neckers, L.5
  • 18
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer, E., and P. Cresswell. 1998. Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16:323-358.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-358
    • Pamer, E.1    Cresswell, P.2
  • 19
    • 0032889431 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase
    • Parkinson, J., S.P. Lees-Miller, and R.D. Everett. 1999. Herpes simplex virus type 1 immediate-early protein Vmw110 induces the proteasome-dependent degradation of the catalytic subunit of DNA-dependent protein kinase. J. Virol. 73:650-657.
    • (1999) J. Virol. , vol.73 , pp. 650-657
    • Parkinson, J.1    Lees-Miller, S.P.2    Everett, R.D.3
  • 20
  • 21
    • 0030849769 scopus 로고    scopus 로고
    • Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody
    • Porgador, A., J.W. Yewdell, Y. Deng, J.R. Bennink, and R.N. Germain. 1997. Localization, quantitation, and in situ detection of specific peptide-MHC class I complexes using a monoclonal antibody. Immunity. 6:715-726.
    • (1997) Immunity. , vol.6 , pp. 715-726
    • Porgador, A.1    Yewdell, J.W.2    Deng, Y.3    Bennink, J.R.4    Germain, R.N.5
  • 22
    • 0028291932 scopus 로고
    • Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors
    • Realini, C., S.W. Rogers, and M. Rechsteiner. 1994. Proposed roles in protein-protein association and presentation of peptides by MHC class I receptors. FEBS Lett. 348:109-113.
    • (1994) FEBS Lett. , vol.348 , pp. 109-113
    • Realini, C.1    Rogers, S.W.2    Rechsteiner, M.3
  • 24
    • 0342813068 scopus 로고    scopus 로고
    • SUMO-1: Wrestling with a new ubiquitin-related modifier
    • Saitoh, H., R.T. Pu, and M. Dasso. 1997. SUMO-1: wrestling with a new ubiquitin-related modifier. Trends Biochem. Sci. 22:374-376.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 374-376
    • Saitoh, H.1    Pu, R.T.2    Dasso, M.3
  • 26
    • 0021235767 scopus 로고
    • Preparation of nuclear matrices from cultured cells: Subfractionation of nuclei in situ
    • Staufenbiel, M., and W. Deppert. 1984. Preparation of nuclear matrices from cultured cells: subfractionation of nuclei in situ. J. Cell Biol. 98:1886-1894.
    • (1984) J. Cell Biol. , vol.98 , pp. 1886-1894
    • Staufenbiel, M.1    Deppert, W.2
  • 28
    • 0020501761 scopus 로고
    • Biology of simian virus 40 (SV40) transplantation antigen (TrAg). IX. Analysis of TrAg in mouse cells synthesizing truncated SV40 large T antigen
    • Tevethia, S., M. Tevethia, A. Lewis, V. Reddy, and S. Weissman. 1983. Biology of simian virus 40 (SV40) transplantation antigen (TrAg). IX. Analysis of TrAg in mouse cells synthesizing truncated SV40 large T antigen. Virology. 128:319-330.
    • (1983) Virology , vol.128 , pp. 319-330
    • Tevethia, S.1    Tevethia, M.2    Lewis, A.3    Reddy, V.4    Weissman, S.5
  • 29
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 30
    • 0024095276 scopus 로고
    • Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen
    • Townsend, A., J. Bastin, K. Gould, G. Brownlee, M. Andrew, B. Coupar, D. Boyle, S. Chan, and G. Smith. 1988. Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen. J. Exp. Med. 168:1211-1224.
    • (1988) J. Exp. Med. , vol.168 , pp. 1211-1224
    • Townsend, A.1    Bastin, J.2    Gould, K.3    Brownlee, G.4    Andrew, M.5    Coupar, B.6    Boyle, D.7    Chan, S.8    Smith, G.9
  • 31
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin α) binding site on the influenza A virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., P. Palese, and R.E. O'Neill. 1997. The NPI-1/NPI-3 (karyopherin α) binding site on the influenza A virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71:1850-1856.
    • (1997) J. Virol. , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 32
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis, K., S. Rambaud, C. Lavau, J. Jansen, T. Carvalho, M. Carmo-Fonseca, A. Lamond, and A. Dejean. 1994. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell. 76:345-356.
    • (1994) Cell. , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejean, A.8
  • 33
    • 0029909097 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis centers in HeLa cells: Indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
    • Wojcik, C., D. Schroeter, S. Wilk, J. Lamprecht, and N. Paweletz. 1996. Ubiquitin-mediated proteolysis centers in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome. Eur. J. Cell Biol. 71:311-318.
    • (1996) Eur. J. Cell Biol. , vol.71 , pp. 311-318
    • Wojcik, C.1    Schroeter, D.2    Wilk, S.3    Lamprecht, J.4    Paweletz, N.5
  • 34
    • 0019411535 scopus 로고
    • Expression of influenza A virus internal antigens on the surface of infected P815 cells
    • Yewdell, J.W., E. Frank, and W. Gerhard. 1981. Expression of influenza A virus internal antigens on the surface of infected P815 cells. J. Immunol 126: 1814-1819.
    • (1981) J. Immunol , vol.126 , pp. 1814-1819
    • Yewdell, J.W.1    Frank, E.2    Gerhard, W.3
  • 35
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York, I., and K.L. Rock. 1996. Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14:369-396.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 369-396
    • York, I.1    Rock, K.L.2
  • 36
    • 0029942879 scopus 로고    scopus 로고
    • Accelerated degradation of PML-retinoic acid receptor alpha (PML-RARA) oncoprotein by all-trans-retinoic acid in acute promyelocytic leukemia: Possible role of the proteasome pathway
    • Yoshida, H., K. Kitamura, K. Tanaka, S. Omura, T. Miyazaki, T. Hachiya, R. Ohno, and T. Naoe. 1996. Accelerated degradation of PML-retinoic acid receptor alpha (PML-RARA) oncoprotein by all-trans-retinoic acid in acute promyelocytic leukemia: possible role of the proteasome pathway. Cancer Res. 56:2945-2948.
    • (1996) Cancer Res. , vol.56 , pp. 2945-2948
    • Yoshida, H.1    Kitamura, K.2    Tanaka, K.3    Omura, S.4    Miyazaki, T.5    Hachiya, T.6    Ohno, R.7    Naoe, T.8
  • 37
    • 0032569794 scopus 로고    scopus 로고
    • Proto-oncogene PML controls genes devoted to MHC class I antigen presentation
    • Zheng, P., Y. Guo, Q. Niu, D.E. Levy, J.A. Dyck, S. Lu, L.A. Sheiman, and Y. Liu. 1998. Proto-oncogene PML controls genes devoted to MHC class I antigen presentation. Nature. 396:373-376.
    • (1998) Nature , vol.396 , pp. 373-376
    • Zheng, P.1    Guo, Y.2    Niu, Q.3    Levy, D.E.4    Dyck, J.A.5    Lu, S.6    Sheiman, L.A.7    Liu, Y.8


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