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Volumn 160, Issue 2, 1998, Pages 788-801

Role of proteasomes in T cell activation and proliferation

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLIN E; PROTEASOME; PROTEINASE INHIBITOR;

EID: 0031985626     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (89)

References (65)
  • 1
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S., and S. Schlender. 1995. Selective protein degradation: a journey's end within the proteasome. Cell 82:881.
    • (1995) Cell , vol.82 , pp. 881
    • Jentsch, S.1    Schlender, S.2
  • 2
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79: 13.
    • (1994) Cell , vol.79 , pp. 13
    • Ciechanover, A.1
  • 3
    • 0019731397 scopus 로고
    • A multicatalytic protease complex from pituitary that forms enkephalin and enkephalin containing peptides
    • Orlowski, M., and S. Wilk. 1981. A multicatalytic protease complex from pituitary that forms enkephalin and enkephalin containing peptides. Biochem. Biophys. Res. Commun. 101:814.
    • (1981) Biochem. Biophys. Res. Commun. , vol.101 , pp. 814
    • Orlowski, M.1    Wilk, S.2
  • 4
    • 0020674228 scopus 로고
    • Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
    • Wilk, S., and M. Orlowski. 1983. Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J. Neurochem. 40:842.
    • (1983) J. Neurochem. , vol.40 , pp. 842
    • Wilk, S.1    Orlowski, M.2
  • 5
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Goldberg. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
    • (1994) Cell , vol.78 , pp. 761
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 6
    • 0028985013 scopus 로고
    • Ubiquitination of the G1 cyclin Cln2p by a Cdc34p-dependent pathway
    • Deshaies, R. J., V. Chau, and M. Kirschner. 1995. Ubiquitination of the G1 cyclin Cln2p by a Cdc34p-dependent pathway. EMBO J. 14:303.
    • (1995) EMBO J. , vol.14 , pp. 303
    • Deshaies, R.J.1    Chau, V.2    Kirschner, M.3
  • 8
    • 0028171039 scopus 로고
    • G1 cyclin degradation: The PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover
    • Salama, S. R., K. B. Hendricks, and J. Thorner. 1994. G1 cyclin degradation: the PEST motif of yeast Cln2 is necessary, but not sufficient, for rapid protein turnover. Mol. Cell. Biol. 14:7953.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7953
    • Salama, S.R.1    Hendricks, K.B.2    Thorner, J.3
  • 9
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • Seufert, W., B. Futcher, and S. Jentsch. 1995. Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature 373:78.
    • (1995) Nature , vol.373 , pp. 78
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 10
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner, M., J. M. Huibregtse, R. D. Vierstra, and P. M. Howley. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495.
    • (1993) Cell , vol.75 , pp. 495
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 12
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78:773.
    • (1994) Cell , vol.78 , pp. 773
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 13
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78:787.
    • (1994) Cell , vol.78 , pp. 787
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 14
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup, M., A. Soza, U. Kuckelkorn, and P. M. Kloetzel. 1996. Peptide antigen production by the proteasome: complexity provides efficiency. Immunol. Today 17:429.
    • (1996) Immunol. Today , vol.17 , pp. 429
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.M.4
  • 15
    • 0028132691 scopus 로고
    • Proteasomes: Protein degradation machines of the cell
    • Peters, J. M. 1994. Proteasomes: protein degradation machines of the cell. Trends Biochem. Sci. 19:377.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 377
    • Peters, J.M.1
  • 16
    • 0027983803 scopus 로고
    • Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease
    • Realini, C., W. Dubiel, G. Pratt, K. Ferrell, and M. Rechsteiner. 1994. Molecular cloning and expression of a γ-interferon-inducible activator of the multicatalytic protease. J. Biol. Chem. 269:20727.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20727
    • Realini, C.1    Dubiel, W.2    Pratt, G.3    Ferrell, K.4    Rechsteiner, M.5
  • 20
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky, A., C. Michaud, J. C. Powers, and M. Orlowski. 1992. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31:9421.
    • (1992) Biochemistry , vol.31 , pp. 9421
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 21
    • 0027421430 scopus 로고
    • Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: A novel catalytic activity in proteasome
    • Tsubuki, S., H. Kawasaki, Y. Saito, N. Miyashita, M. Inomata, and S. Kawashima. 1993. Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome. Biochem. Biophys. Res. Commun. 196:1195.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1195
    • Tsubuki, S.1    Kawasaki, H.2    Saito, Y.3    Miyashita, N.4    Inomata, M.5    Kawashima, S.6
  • 24
    • 0026011974 scopus 로고
    • Structure of lactacystin, a new microbial metabolite which induces differentiation of neuroblastoma cells
    • Omura, S., K. Matsuzaki, T. Fujimoto, K. Kosuge, T. Furuya, S. Fijita, and A. Nakagawa. 1991. Structure of lactacystin, a new microbial metabolite which induces differentiation of neuroblastoma cells. J. Antibiot. 44:117.
    • (1991) J. Antibiot. , vol.44 , pp. 117
    • Omura, S.1    Matsuzaki, K.2    Fujimoto, T.3    Kosuge, K.4    Furuya, T.5    Fijita, S.6    Nakagawa, A.7
  • 25
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:72.
    • (1995) Science , vol.268 , pp. 72
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 28
    • 0027424954 scopus 로고
    • Anti-CD28 antibody-and IL-4-induced human T cell proliferation is sensitive to rapamycin
    • Luo, H., H. Chen, P. Daloze, G. St-Louis, and J. Wu. 1993. Anti-CD28 antibody-and IL-4-induced human T cell proliferation is sensitive to rapamycin. Clin. Exp. Immunol. 94:371.
    • (1993) Clin. Exp. Immunol. , vol.94 , pp. 371
    • Luo, H.1    Chen, H.2    Daloze, P.3    St-Louis, G.4    Wu, J.5
  • 29
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNa fragmentation during apoptosis
    • Liu, X., H. Zou, C. Slaughter, and X. Wang. 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175.
    • (1997) Cell , vol.89 , pp. 175
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 30
    • 0023152576 scopus 로고
    • Establishment of propagatable epithelial cell lines from normal adult rat pancreas
    • Tsao, M. S., and M. P. Duguid. 1987. Establishment of propagatable epithelial cell lines from normal adult rat pancreas. Exp. Cell Res. 168:365.
    • (1987) Exp. Cell Res. , vol.168 , pp. 365
    • Tsao, M.S.1    Duguid, M.P.2
  • 31
    • 0028242752 scopus 로고
    • Expression of a G-protein β subunit-related gene during lymphocyte activation
    • Shan, X., H. Luo, B. Houle, and J. Wu. 1994. Expression of a G-protein β subunit-related gene during lymphocyte activation. Int. Immunol. 6:739.
    • (1994) Int. Immunol. , vol.6 , pp. 739
    • Shan, X.1    Luo, H.2    Houle, B.3    Wu, J.4
  • 33
    • 0030598885 scopus 로고    scopus 로고
    • A signaling pathway to translational control
    • Brown, E. J., and S. L. Schreiber. 1996. A signaling pathway to translational control. Cell 86:517.
    • (1996) Cell , vol.86 , pp. 517
    • Brown, E.J.1    Schreiber, S.L.2
  • 34
    • 0028128954 scopus 로고
    • Differential expression and regulation of cyclin D1 protein in normal and tumor human cells: Association with Cdk4 is required for cyclin D1 function in G1 progression
    • Tam, S. W., A. M. Theodoras, J. W. Shay, G. F. Draetta, and M. Pagano. 1994. Differential expression and regulation of cyclin D1 protein in normal and tumor human cells: association with Cdk4 is required for cyclin D1 function in G1 progression. Oncogene 9:2663.
    • (1994) Oncogene , vol.9 , pp. 2663
    • Tam, S.W.1    Theodoras, A.M.2    Shay, J.W.3    Draetta, G.F.4    Pagano, M.5
  • 35
    • 0028999777 scopus 로고
    • Cyclin D2 is a moderately oscillating nucleoprotein required for G1 phase progression in specific cell types
    • Lukas, J., J. Bartkova, M. Welcker, O. W. Petersen, G. Peters, M. Strauss, and J. Bartek. 1995. Cyclin D2 is a moderately oscillating nucleoprotein required for G1 phase progression in specific cell types. Oncogene 10:2125.
    • (1995) Oncogene , vol.10 , pp. 2125
    • Lukas, J.1    Bartkova, J.2    Welcker, M.3    Petersen, O.W.4    Peters, G.5    Strauss, M.6    Bartek, J.7
  • 36
    • 0027742184 scopus 로고
    • Distinct roles for cyclin-dependent kinases in cell cycle control
    • Van der Heuvel, S., and E. Harlow. 1993. Distinct roles for cyclin-dependent kinases in cell cycle control. Science 262:2050.
    • (1993) Science , vol.262 , pp. 2050
    • Van Der Heuvel, S.1    Harlow, E.2
  • 37
    • 0027336491 scopus 로고
    • Mammalian G1 cyclins
    • Sherr, C. J. 1993. Mammalian G1 cyclins. Cell 73:1059.
    • (1993) Cell , vol.73 , pp. 1059
    • Sherr, C.J.1
  • 38
    • 0026583746 scopus 로고
    • Cyclin a is required at two points in the human cell cycle
    • Pagano, M., R. Pepperkok, F. Verde, W. Ansorge, and G. Draetta. 1992. Cyclin A is required at two points in the human cell cycle. EMBO J. 11:961.
    • (1992) EMBO J. , vol.11 , pp. 961
    • Pagano, M.1    Pepperkok, R.2    Verde, F.3    Ansorge, W.4    Draetta, G.5
  • 39
    • 0028875086 scopus 로고
    • Evidence for different modes of action of cyclin-dependent kinase inhibitors: p15 and p16 bind to kinases, p21 and p27 bind to cyclins
    • Hall, M., S. Bates, and G. Peters. 1995. Evidence for different modes of action of cyclin-dependent kinase inhibitors: p15 and p16 bind to kinases, p21 and p27 bind to cyclins. Oncogene 11:1581.
    • (1995) Oncogene , vol.11 , pp. 1581
    • Hall, M.1    Bates, S.2    Peters, G.3
  • 41
    • 0029670477 scopus 로고    scopus 로고
    • Kip1 accumulation during the cell cycle
    • Kip1 accumulation during the cell cycle. Science 271:1861.
    • (1996) Science , vol.271 , pp. 1861
    • Hengst, L.1    Reed, S.I.2
  • 43
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: A central role for clasto-lactacystin β-lactone
    • Dick, L. R., A. A. Cruikshank, L. Grenier, F. D. Melandri, S. L. Nunes, and R. L. Stein. 1996. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin β-lactone. J. Biol. Chem. 271: 7273.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7273
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 48
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer, M., A. Murray, and M. Kirschner. 1991. Cyclin is degraded by the ubiquitin pathway. Nature 349:132.
    • (1991) Nature , vol.349 , pp. 132
    • Glotzer, M.1    Murray, A.2    Kirschner, M.3
  • 49
    • 0026459047 scopus 로고
    • D type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA
    • Xiong, Y., H. Zhang, and D. Beach. 1992. D type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA. Cell 71:505.
    • (1992) Cell , vol.71 , pp. 505
    • Xiong, Y.1    Zhang, H.2    Beach, D.3
  • 50
    • 0027425599 scopus 로고
    • Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system
    • Tsai, L. H., T. Takahashi, V. S. Caviness, Jr., and E. Harlow. 1993. Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system. Development 119:1029.
    • (1993) Development , vol.119 , pp. 1029
    • Tsai, L.H.1    Takahashi, T.2    Caviness Jr., V.S.3    Harlow, E.4
  • 51
    • 0029737650 scopus 로고    scopus 로고
    • Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E
    • Won, K. A., and S. I. Reed. 1996. Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15:4182.
    • (1996) EMBO J. , vol.15 , pp. 4182
    • Won, K.A.1    Reed, S.I.2
  • 52
    • 0027752979 scopus 로고
    • A link between cyclin A expression and adhesion-dependent cell cycle progression
    • Guadagno, T. J., M. Obtsubo, J. M. Roberts, and R. K. Assoian. 1993. A link between cyclin A expression and adhesion-dependent cell cycle progression. Science 262:1572.
    • (1993) Science , vol.262 , pp. 1572
    • Guadagno, T.J.1    Obtsubo, M.2    Roberts, J.M.3    Assoian, R.K.4
  • 53
    • 0028168242 scopus 로고
    • Ink4B is a potential effector of TGF-β-induced cell cycle arrest
    • Ink4B is a potential effector of TGF-β-induced cell cycle arrest. Nature 371:257.
    • (1994) Nature , vol.371 , pp. 257
    • Hannon, G.J.1    Beach, D.2
  • 55
    • 0029851287 scopus 로고    scopus 로고
    • Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1
    • Hirai, H., and C. J. Sherr. 1996. Interaction of D-type cyclins with a novel myb-like transcription factor, DMP1. Mol. Cell. Biol. 16:6457.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6457
    • Hirai, H.1    Sherr, C.J.2
  • 56
    • 0028171292 scopus 로고
    • G1 phase progression: Cycling on cue
    • Sherr, C. J. 1994. G1 phase progression: cycling on cue. Cell 79:551.
    • (1994) Cell , vol.79 , pp. 551
    • Sherr, C.J.1
  • 57
    • 0028229732 scopus 로고
    • Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes
    • Firpo, E. J., A. Koff, M. J. Solomon, and J. M. Roberts. 1994. Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes. Mol. Cell. Biol. 14:4889.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4889
    • Firpo, E.J.1    Koff, A.2    Solomon, M.J.3    Roberts, J.M.4
  • 59
    • 0027371861 scopus 로고
    • Rapamycin inhibition of interleukin-2-dependent p33 (CDK2) and p34 (CDC2) kinase activation in T lymphocytes
    • Morice, W. G., G. Wiederrecht, G. J. Brunn, J. J. Siekierka, and R. T. Abraham. 1993. Rapamycin inhibition of interleukin-2-dependent p33 (CDK2) and p34 (CDC2) kinase activation in T lymphocytes. J. Biol. Chem. 268:22737.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22737
    • Morice, W.G.1    Wiederrecht, G.2    Brunn, G.J.3    Siekierka, J.J.4    Abraham, R.T.5
  • 61
    • 0028337685 scopus 로고
    • Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro
    • Waga, S., and B. Stillman. 1994. Anatomy of a DNA replication fork revealed by reconstitution of SV40 DNA replication in vitro. Nature 369:207.
    • (1994) Nature , vol.369 , pp. 207
    • Waga, S.1    Stillman, B.2
  • 62
    • 0028169236 scopus 로고
    • p21-containing cyclin kinases exist in both active and inactive states
    • Zhang, H., G. J. Hannon, and D. Beach. 1994. p21-containing cyclin kinases exist in both active and inactive states. Genes Dev. 8:1750.
    • (1994) Genes Dev. , vol.8 , pp. 1750
    • Zhang, H.1    Hannon, G.J.2    Beach, D.3
  • 65
    • 0027330043 scopus 로고
    • The role of NF-kappa B1 (p50/p105) gene expression in activation of human blood T-lymphocytes via CD2 and CD28 adhesion molecules
    • Costello, R., C. Cerdan, C. Lipcey, M. Algarte, Y. Martin, P. A. Baeuerle, D. Olive, and J. Imbert. 1993. The role of NF-kappa B1 (p50/p105) gene expression in activation of human blood T-lymphocytes via CD2 and CD28 adhesion molecules. Cell Growth Differ. 4:947.
    • (1993) Cell Growth Differ. , vol.4 , pp. 947
    • Costello, R.1    Cerdan, C.2    Lipcey, C.3    Algarte, M.4    Martin, Y.5    Baeuerle, P.A.6    Olive, D.7    Imbert, J.8


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