Proteasomes: Structure and biology

Journal of Biochemistry

Volumn 123, Issue 2, 1998, Pages 195-204

  Tanaka, Keiji ^a  

^a JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

20S and 26S proteasomes; ATP dependent proteolysis; PA28; PA700; Ubiquitin

Indexed keywords

CALPAIN; CALPASTATIN; CELL PROTEIN; INTERFERON; PROTEASOME; PROTEINASE; PROTEINASE INHIBITOR; REGULATOR PROTEIN; UBIQUITIN;

CELL CYCLE; COMPLEX FORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE; IMMUNE RESPONSE; PROTEIN DEGRADATION; PROTEIN INDUCTION; PROTEIN QUALITY; REVIEW; SIGNAL TRANSDUCTION;

EID: 0031887332     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021922     Document Type: Review

References (80)

1. Hershko, A. (1997) Lessons from the discovery of the ubiquitin system. Trend. Biochem. Sci. 21, 445-449
2. Tanaka, K., Waxman, L., and Goldberg, A. (1983) ATP serves two distinct roles in protein degradation in reticulocytes. One requiring and one independent of ubiquitin. J. Cell Biol. 96, 1580-1585
3. Coux, O., Tanaka, K., and Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847
4. Rechsteiner, M., Hoffman, L., and Dubiel, W. (1993) The multicatalytic and 26S proteases. J. Biol. Chem. 268, 6065-6068
5. Hochstrasser, M. (1997) Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30, 405-439
6. Varshavsky, A. (1997) The N-end rule pathway of protein degradation. Genes Cells 2, 13-28
7. Baumeister, W. and Lupas, A. (1997) The proteasome. Curr. Opin. Struct. Biol. 7, 273-278
8. Groll, M., Ditzel, L., Lowe, J., Stock, D., Bochtler, M., Bartunik, H.D., and Huber, R. (1997) Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386, 463-471
9. van Nocker, S., Deveraux, Q., Rechsteiner, M., and Vierstra, R. (1996) Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. USA 93, 856-860
10. van Nocker, S., Sadis, S., Rubin, D.M., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., and Vierstra, R.D. (1996) The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a non-essential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028
11. Kominami, K., Okura, N., Kawamura, M., DeMartino, G.N., Slaughter, C.A., Shimbara, N., Chung, C.H., Fujimuro, M., Yokosawa, H., Shimizu, Y., Tanahashi, N., Tanaka, K., and Toh-e, A. (1997) Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1. Mol. Biol. Cell 8, 171-187
12. Lam, Y.A., Xu, W., DeMartino, G.N., and Cohen, R.E. (1997) Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature 385, 737-740
13. Ma, C.-P., Slaughter, C.A., and DeMartino, G.N. (1992) Identification, purification, and characterization of a protein activator (PA28) of the 20S proteasome (macropain). J. Biol. Chem. 267, 10515-10523
14. Gray, C.W., Slaughter, C.A., and DeMartino, G.N. (1994) PA28 activator protein forms regulatory caps on proteasome stacked rings. J. Mol. Biol. 236, 7-15
15. Ahn, J.Y., Tanahashi, N., Akiyama, K., Hisamatsu, H., Noda, C., Tanaka, K., Chung, C.H., Shimbara, N., Willy, P.J., Mott, J.D., Slaughter, C.A., and DeMartino, G.N. (1995) Primary structures of two homologous subunits of PA28, a γ-interferon-inducible protein activator of the 20S proteasome. FEBS Lett. 366, 37-42
16. Tanahashi, N., Yokota, K., Ahn, J.N., Chung, C.H., Fujiwara, T., Takahashi, E., DeMartino, G.N., Slaughter, C.A., Toyonaga, T., Yamamura, K., Shimbara, N., and Tanaka, K. (1997) Molecular properties of the proteasome activator PA28 family proteins and γ-interferon regulation. Genes Cells 2, 195-211
17. Realini, C., Jensen, C.C., Zhang, Z., Johnsto, S.C., Knowlton, J.R., Hill, C.P., and Rechsteiner, M. (1997) Characterization of recombinant REGα, REGβ, and REGγ proteasome activators. J. Biol. Chem. 272, 25483-25492
18. Soza, A., Knuehl, C., Groettrup, M., Henkliein, P., Tanaka, K., and Kloetzel, P.-M. (1997) Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett. 413, 27-34
19. Hilt, W. and Wolf, D.H. (1995) Proteasomes: destruction as a programme. Trends Biochem. Sci. 21, 96-102
20. Omura, S., Fujimoto, T., Otoguro, K., Matsuzaki, K., Moriguchi, R., Tanaka, H., and Sasaki, Y. (1991) Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J. Antibiot. 44, 113-116
21. Fenteany, G., Standaert, R.F., Lane, W.S., Choi, S., Corey, E.J., and Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-acid terminal threonine modification by lactacystin. Science 268, 726-731
22. Dick, L.R., Cruikshank, A.A., Destree, A.T., Grenier, L., McCormack, T.A., Melandri, F.D., Nunes, S.L., Palombella, V.J., Parent, L.A., Plamondon, L., and Stein, R.L. (1997) Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J. Biol. Chem. 272, 182-188
23. Cardozo, C., Vinitsky, A., Hidalgo, M.C., Michaud, C., and Orlowski, M. (1992) A 3,4-dichloroisocoumarin-resistant component of the multicatalytic proteinase complex. Biochemistry 31, 7373-7380
24. Bogyo, M., McMaster, J.S., Gaczynska, M., Tortorella, D., Goldberg, A.L., and Ploegh, H. (1997) Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94, 6629-6634
25. Vinitsky, A., Cardozo, C., Sepp-Lorenzino, L., Michaud, C., and Orlowski, M. (1994) Inhibition of the proteolytic activity of the multicatalytic proteinase complex (proteasome) by substrate-related peptidyl aldehydes. J. Biol. Chem. 47, 29860-29866
26. Traenckner, E.B.-M., Wilk, S., and Baeuerle, P.A. (1994) A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB. EMBO J. 13, 5433-5441
27. Jensen, T.J., Loo, M.A., Pind, S., Williams, D.B., Goldberg, A.L., and Riordan, J.R. (1995) Multiple proteolytic systems, including the proteasome contribute to CFTR processing. Cell 83, 129-135
28. Tsubuki, S., Saito, Y., Tomioka, M., Ito, H., and Kawashima, S. (1996) Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J. Biochem. 119, 572-576
29. Rock, K.L., Gramm, C., Rothstein, L., Clark, K., Stein, R., Dick, L., Hwang, D., and Goldberg, A.L. (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, 761-771
30. Figueiredo-Pereira, M.E., Banik, N., and Wilk, S. (1994) Comparison of the effect of calpain inhibitors on two extralysosomal proteinases: The multicatalytic proteinase complex and m-calpain. J. Neurochem. 62, 1989-1994
31. Tanaka, K. and Tanahashi, N. (1997) The 20S proteasome: subunits and functions. Adv. Mol. Cell. Biol. in press
32. Deshaies, R.J., Chau, V., and Kirschner, M. (1995) Ubiquitination of the G1 cyclin Cln2p by a Cdc34p-dependent pathway. EMBO J. 14, 303-312
33. Yaglom, J.A., Goldberg, A.L., Finley, D., and Sherman, M.Y. (1996) The molecular chaperone Ydj1 is required for the p34-CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation. Mol. Cell. Biol. 16, 3679-3684
34. Won, K.-A. and Reed, S.I. (1996) Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. EMBO J. 15, 4182-4193
35. Diehl, J.A., Zindy, F., and Sherr, C.J. (1997) Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev. 11, 957-972
36. Funabiki, H., Yamano, H., Kumada, K., Nagano, K., Hunt, T., and Yanagida, M. (1996) Cut2 proteolysis required for sister-chromatid separation in fission yeast. Nature 381, 438-441
37. K1p1. Genes Dev. 11, 1464-1478
38. Verma, R., Feldman, R.M.R., and Deshaies, R. J. (1997) SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34 and cyclin/CDK4 activities. Mol. Biol. Cell 8, 1427-1437
39. Kominami, K. and Toda, T. (1997) Fission yeast WD-repeat protein Pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18. Genes Dev. 11, 1548-1560
40. Chen, Z., Hagler, J., Palombella, V. J., Melandri, F., Scherer, D., Ballard, D., and Maniatis, T. (1995) Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev. 9, 1586-1597
41. Kim, T.K. and Maniatis, T. (1996) Regulation of interferon-gamma-activated STAT1 by the ubiquitin-proteasome pathway. Science 273, 1717-1719
42. Yamin, T.-T. and Miller, D.K. (1997) The interleukin-1 receptor-associated kinase is degraded by proteasomes following its phosphorylation. J. Biol. Chem. 272, 21540-21547
43. Aberie, H., Bauer, A., Stappert, J., Kispert, A., and Kemler, R. (1998) β-Catenin is a target of the ubiquitin-proteasome pathway. EMBO J. 16, 3797-3804
44. Rechsteiner, M. and Rogers, S.W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21, 267-271
45. Nishizawa, M., Okazaki, K., Furuno, N., Watanabe, N., and Sagata, N. (1992) The 'second-codon rule' and autophosphorylation govern the stability and activity of Mos during the meiotic cell cycle in Xenopus oocytes. EMBO J. 11, 2433-2466
46. Okazaki, K. and Sagata, N. (1996) The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and auguments its transforming activity in NIH 3T3 cells. EMBO J. 14, 5048-5059
47. Musti, A.M., Treier, M., and Bohmann, D. (1997) Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275, 400-402
48. Glotzer, M., Murray, A.W., and Kirschner, M.W. (1991) Cyclin is degraded by the ubiquitin pathway. Nature 349, 132-138
49. Hershko, A. (1997) Roles of ubiquitin-dependent proteolysis in cell cycle control. Curr. Opin. Cell. Biol. 9, 788-799
50. Cohen-Fix, O., Peters, J.-M., Kirschner, M.W., and Koshland, D. (1996) Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p. Genes Dev. 10, 3081-3093
51. Juang, Y.-L., Huang, J., Peters, J.-M., McLaughlin, M. E., Tai, C.-Y., and Pellman, D. (1997) APC-mediated proteolysis of Ase1 and the morphogenesis of the mitotic spindle. Science 275, 1311-1314
52. Ghislain, M., Udvardy, A., and Mann, C. (1993) S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366, 358-362
53. Gordon, C., McGurk, G., Dillon, P., Rosen, C., and Hastie, N.D. (1993) Defective mitosis due to a mutation in the gene for a fission yeast 26S protease subunit. Nature 366, 3655-3657
54. Kominami, K., DeMartino, G.N., Moomaw, C.R., Slaughter, C.A., Shimbara, N., Fujimuro, M., Yokosawa, H., Hisamatsu, H., Tanahashi, N., Shimizu, Y., Tanaka, K., and Toh-e, A. (1995) Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. EMBO J. 14, 3105-3115
55. Scheffner, M., Nuber, U., and Huibregtse, J.M. (1995) Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373, 81-83
56. Huibregtse, J.M., Sxheffner, M., Beaudeon, S., and Howley, P.M. (1995) A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. USA 92, 2563-2567
57. Haupt, Y., Maya, R., and Oren, M. (1997) Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299
58. Chang, Y-C., Lee, Y.-S., Tejima, T., Tanaka, K., Omura, S., Heintz, N.H., Mitsui, Y., and Magae, J. (1997) Degradation of -p53 responsive proteins, Bax and Mdm-2 by ubiquitin/proteasome proteolytic system. Cell Growth Differ. in press
59. DiDonato, J.A., Hayakawa, M., Rothwarf, D.M., Zandi, E., and Karin, M. (1997) A cytokine-responsive IκB kinase that activates the transcription factor NF-κB. Nature 388, 548-554
60. Mori, S., Tanaka, K., Omura, S., and Saito, Y. (1995) Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves the ubiquitin-proteasome proteolytic pathway. J. Biol. Chem. 270, 29447-29452
61. Jeffers, M., Taylor, G.A., Weidner, K.M., Omura, S., and Vande Woude, G.F. (1997) Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell. Biol. 17, 799-808
62. Biederer, T., Volkswein, C., and Sommer, T. (1996) Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15, 2069-2076
63. McGee, T.P., Cheng, H.H., Kumagai, H., Omura, S., and Simoni, R.D. (1996) Degradation of 3-hydroxyl-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as result of increased susceptibility to proteolysis. J. Biol. Chem. 271, 25630-25638
64. Wu, X., Sakata, N., Lele, K.M., Zhou, M., Jiang, H., and Ginsberg, H.N. (1997) A two-site model for ApoB degradation in HepG2 cells. J. Biol. Chem. 272, 11575-11580
65. Guo, B., Phillips, J.D., Yu, Y., and Leibold, E.A. (1995) Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 270, 21645-21651
66. Schneider, C., Sepp-Lorenzino, L., Nimmesgern, E., Ouerfelli, O., Danishefsky, S., Rosen, N., and Hartl, F.U. (1996) Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90. Proc. Natl. Acad. Sci. USA 93, 14536-14541
67. Kopito, R.R. (1997) ER quality control: The cytoplasmic connection. Cell 88, 427-430
68. Brodsky, J.L. and McCracken, A.A. (1997) ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-156
69. Murakami, Y., Matsufuji, S., Kameji, T., Hayashi, S., Igarashi, K., Tamura, T., Tanaka, K., and Ichihara, A. (1992) Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360, 597-599
70. Jariel-Encontre, I., Pariat, M., Martin, F., Carillo, S., Salvat, C., and Piechaczyk, M. (1995) Ubiquitinylation is not an absolute requirement for degradation of c-Jun protein by the 26 S proteasome. J. Biol. Chem. 270, 11623-11627
71. Geoffrey, H.Y., Kaung, G., Kobayashi, S., and Kopito, R.R. (1997) Cytoplasmic degradation of T-cell receptor α chain by the proteasome. J. Biol. Chem. 272, 20800-20804
72. Palombella, V.J., Rando, O.J., Goldberg, A.L., and Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for pro-cessing the NF-κ B1 precursor protein and the activation of NF-κB. Cell 78, 773-785
73. Lin, L. and Ghosh, S. (1996) A glycine-rich region in NF-κB p105 functions as a processing signal for the generation of the p50 subunit. Mol. Cell. Biol. 16, 2248-2254
74. York, I.A. and Rock, K.L. (1996) Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14, 369-397
75. Groettrup, M., Soza, A., Kuckelkorn, U., and Kloetzel, P.M. (1996) Peptide antigen production by the proteasome: complexity provides efficiency. Immunol. Today 17, 429-435
76. Tanaka, K., Tanahashi, N., Tsurumi, C., Yokota, K., and Shimbara, N. (1997) Proteasomes and antigen processing. Adv. Immunol. 64, 1-38
77. Kasahara, M., Hayashi, M., Tanaka, K., Inoko, H., Sugaya, K., Ikemura, T., and Ishibashi, T. (1996) Chromosomal localization of the proteasome Z gene reveals an ancient chromosomal duplication involving the major histocompatibility complex. Proc. Natl. Acad. Sci. USA 93, 9096-9101
78. Groettrup, M., Soza, A., Eggers, M., Kuehn, L., Dick, T.P., Schild, H., Rammensee, H.-G., Koszinowski, U., and Kloetzel, P.-M. (1996) A role of the proteasome regulator PA28α in antigen presentation. Nature 381, 166-168
79. Dick, T.P., Ruppert, T., Groettrup, M., Kloetzel, P.M., Kuehn, L., Koszinowski, U.H., Stevanovic, S., Schild, H., and Rammensee, H-G. (1996) Coordinated dual cleavages induced by the proteasome regulator PA28 lead to dominant MHC ligands. Cell 86, 253-262
80. Shimbara, N., Nakajima, H., Tanahashi, N., Ogawa, K., Niwa, S., Uenaka, A., Nakayama, E., and Tanaka, K. (1998) Double-cleavage production of the CTL epitope by proteasomes and PA28: role of the flanking region. Genes to Cells, in press