The 26S Proteasome

Protein Degradation

Volumn 1, Issue , 2007, Pages 220-247

  Rechsteiner, Martin ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

20S proteasome; 26S proteasome; Physiological aspects; Proteasome activators; Proteasome biogenesis; Protein degradation; Protein inhibitors of the proteasome; Proteolysis by the 26S proteasome; Substrate recognition by proteasomes

Indexed keywords

EID: 69949122631     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527619320.ch9     Document Type: Chapter

References (174)

1. Reed, S. I. Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover. Nat Rev Mol Cell Biol 2003, 4, 855-64.
2. Bashir, T. and Pagano, M. Aberrant ubiquitin-mediated proteolysis of cell cycle regulatory proteins and oncogenesis. Adv Cancer Res 2003, 88, 101-44.
3. Vierstra, R. D. The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci 2003, 8, 135-42.
4. Campbell, D. S. and Holt, C. E. Chemotropic responses of retinal growth cones mediated by rapid local protein synthesis and degradation. Neuron 2001, 32, 1013-1026.
5. Hegde, A. N. and DiAntonio, A. Ubiquitin and the synapse. Nat Rev Neurosci 2002, 3, 854-61.
6. Muratani, M. and Tansey, W. P. How the ubiquitin-proteasome system controls transcription. Nat Rev Mol Cell Biol 2003, 4, 192-201.
7. Conaway, R. C., Brower, C. S., and Conaway, J. W. Emerging roles of ubiquitin in transcription regulation. Science 2002, 296, 1254-8.
8. Lipford, J. R. and Deshaies, R. J. Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation. Nat Cell Biol 2003, 5, 845-50.
9. Seeler, J. S. and Dejean, A. Nuclear and unclear functions of SUMO. Nat Rev Mol Cell Biol 2003, 4, 690-9.
10. Schwartz, D. C. and Hochstrasser, M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci 2003, 28, 321-8.
11. Jason, L. J., Moore, S. C., Lewis, J. D., Lindsey, G., and Ausio, J. Histone ubiquitination: a tagging tail unfolds? Bioessays 2002, 24, 166-74.
12. Zhang, Y. Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev 2003, 17, 2733-40.
13. Deng, L. et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitinconjugating enzyme complex and a unique polyubiquitin chain. Cell 2000, 103, 351-361.
14. Hicke, L. and Dunn, R. Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins. Annu Rev Cell Dev Biol 2003, 19, 141-72.
15. Pornillos, O., Garrus, J. E., and Sundquist, W. I. Mechanisms of enveloped RNA virus budding. Trends Cell Biol 2002, 12, 569-79.
16. Hershko, A., Ciechanover, A., and Varshavsky, A. Basic Medical Research Award. The ubiquitin system. Nat Med 2000, 6, 1073-81.
17. Kessel, M. et al. Homology in structural organization between E. coli ClpAP protease the eukaryotic 26S proteasome. J Mol Biol 1995, 250, 587-594.
18. Lowe, J. et al. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science 1995, 268, 533-539.
19. Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997, 386, 463-471.
20. Unno, M. et al. The structure of the mammalian 20S proteasome at 2.75 A resolution. Structure (Camb) 2002, 10, 609-18.
21. Dahlmann, B. et al. The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme. Biomed Biochim Acta 1991, 50, 465-9.
22. Harris, J. L., Alper, P. B., Li, J., Rechsteiner, M., and Backes, B. J. Substrate specificity of the human proteasome. Chem Biol 2001, 8, 1131-41.
23. Seemuller, E. et al. Proteasome from Thermoplasma acidophilum: a threonine protease. Science 1995, 268, 579-582.
24. Fenteany, G. et al. Inhibition of proteasome activities and subunitspecific amino-terminal threonine modification by lactacystin. Science 1995, 268, 726-731.
25. Meng, L. et al. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity. Proc. Natl. Acad. Sci. USA 1999, 96, 10403-10408.
26. Bogyo, M. et al. Covalent modification of the active site threonine of proteasomal b subunits and the Escherichia coli homolg HsIV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 1997, 94, 6629-6634.
27. Kane, R. C., Bross, P. F., Farrell, A. T., and Pazdur, R. Velcade: U.S. FDAapproval for the treatment of multiple myeloma progressing on prior therapy. Oncologist 2003, 8, 508-13.
28. Yewdell, J. W. and Hill, A. B. Viral interference with antigen presentation. Nat Immunol 2002, 3, 1019-25.
29. Goldberg, A. L., Cascio, P., Saric, T., and Rock, K. L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol Immunol 2002, 39, 147-64.
30. Rammensee, H.-G., Falk, K., and Rötzschke, O. Peptides naturally presented by MHC class I molecules. Annu. Rev. Immunol. 1993, 11, 213-244.
31. Dougan, D. A., Mogk, A., Zeth, K., Turgay, K., and Bukau, B. AAA{thorn} proteins and substrate recognition, it all depends on their partner in crime. FEBS Lett 2002, 529, 6-10.
32. Peters, J. M., Cejka, Z., Harris, J. R., Kleinschmidt, J. A., and Baumeister, W. Structural features of the 26S proteasome complex. J Mol Biol 1993, 234, 932-937.
33. Walz, J. et al. 26S proteasome structure revealed by three-dimensional electron microscopy. J Struct Biol 1998, 121, 19-29.
34. Glickman, M. H. et al. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and elF3. Cell 1998, 94, 615-623.
35. Kapelari, B. et al. Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. J Mol Biol 2000, 300, 1169-78.
36. Rechsteiner, M., Hoffman, L., and Dubiel, W. The multicatalytic and 26S proteases. J. Biol. Chem. 1993, 268, 6065-6068.
37. Richmond, C., Gorbea, C., and Rechsteiner, M. Specific interactions between ATPase subunits of the 26S protease. J. Biol. Chem. 1997, 272, 13403-13411.
38. Rubin, D. M., Glickman, M. H., Larsen, C. N., Dhruvakumar, S., and Finley, D. Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J. 1998, 17, 4909-4919.
39. Davey, M. J., Jeruzalmi, D., Kuriyan, J., and O'Donnell, M. Motors and switches: AAA{thorn} machines within the replisome. Nat Rev Mol Cell Biol 2002, 3, 826-35.
40. Lee, S. Y. et al. Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA{thorn} ATPase domains. Genes Dev 2003, 17, 2552-63.
41. Hartmann-Petersen, R., Tanaka, K., and Hendil, K. B. Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking. Arch Biochem Biophys 2001, 386, 89-94.
42. Berndt, C., Bech-Otschir, D., Dubiel, W., and Seeger, M. Ubiquitin system: JAMMing in the name of the lid. Curr Biol 2002, 12, R815-7.
43. Cope, G. A. and Deshaies, R. J. COP9 signalosome: a multifunctional regulator of SCF and other cullinbased ubiquitin ligases. Cell 2003, 114, 663-71.
44. Li, L. and Deng, X. W. The COP9 signalosome: an alternative lid for the 26S proteasome? Trends Cell Biol 2003, 13, 507-9.
45. Ferrell, K., Wilkinson, C. R., Dubiel, W., and Gordon, C. Regulatory subunit interactions of the 26S proteasome, a complex problem. Trends Biochem Sci 2000, 25, 83-8.
46. Fu, H., Reis, N., Lee, Y., Glickman, M. H., and Vierstra, R. D. Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome. Embo J 2001, 20, 7096-107.
47. Cagney, G., Uetz, P., and Fields, S. Two-hybrid analysis of the Saccharomyces cerevisiae 26S proteasome. Physiol Genomics 2001, 7, 27-34.
48. Davy, A. et al. A protein-protein interaction map of the Caenorhabditis elegans 26S proteasome. EMBO Rep 2001, 2, 821-8.
49. Cope, G. A. et al. Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 2002, 298, 608-11.
50. Bailly, E. and Reed, S. I. Functional characterization of rpn3 uncovers a distinct 19S proteasomal subunit requirement for ubiquitin-dependent proteolysis of cell cycle regulatory proteins in budding yeast. Mol Cell Biol 1999, 19, 6872-90.
51. Fong, A., Zhang, M., Neely, J., and Sun, S. C. S9, a 19 S proteasome subunit interacting with ubiquitinated NF-kappaB2/p100. J Biol Chem 2002, 277, 40697-702.
52. Deveraux, Q., Ustrell, V., Pickart, C., and Rechsteiner, M. A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 1994, 269, 7059-7061.
53. van Nocker, S. et al. The Multiubiquitin-Chain-Binding Protein Mcb1 Is a Component of the 26S Proteasome in Saccharomyces cerevisiae and Plays a Nonessentail, Substrate-Specific Role in Protein Turnover. Mol. Cell Biol. 1996, 16, 6020-6028.
54. Kajava, A. V. What curves alphasolenoids? Evidence for an alphahelical toroid structure of Rpn1 and Rpn2 proteins of the 26S proteasome. J Biol Chem 2002, 277, 49791-8.
55. Elsasser, S. et al. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol 2002, 4, 725-30.
56. Saeki, Y., Sone, T., Toh-e, A., and Yokosawa, H. Identification of ubiquitin-like protein-binding subunits of the 26S proteasome. Biochem Biophys Res Commun 2002, 296, 813-9.
57. Lam, Y. A., Lawson, T. G., Velayutham, M., Zweier, J. L., and Pickart, C. M. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 2002, 416, 763-7.
58. Hoffman, L. and Rechsteiner, M. Activation of the multicatalytic protease. The 11 S regulator and 20S ATPase complexes contain distinct 30-kilodalton subunits. J. Biol. Chem. 1994, 269, 16890-16895.
59. Braun, B. C. et al. The base of the proteasome regulatory particle exhibits chaperone-like activity. Nat Cell Biol 1999, 1, 221-6.
60. Strickland, E., Hakala, K., Thomas, P. J., and DeMartino, G. N. Recognition of misfolding proteins by PA700, the regulatory subcomplex of the 26S proteasome. J Biol Chem 2000, 275, 5565-72.
61. Liu, C. W. et al. Conformational remodeling of proteasomal substrates by PA700, the 19 S regulatory complex of the 26S proteasome. J Biol Chem 2002, 277, 26815-20.
62. Gonzalez, F., Delahodde, A., Kodadek, T., and Johnston, S. A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 2002, 296, 548-50.
63. Hoffman, L., Pratt, G., and Rechsteiner, M. Multiple forms of the 20 S multicatalytic and the 26S ubiquitin/ATP-dependent proteases from rabbit reticulocyte lysate. J. Biol. Chem. 1992, 267, 22362-22368.
64. Verma, R. et al. Proteasomal proteomics: identification of nucleotidesensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 2000, 11, 3425-39.
65. Guterman, A. and Glickman, M. H. Complementary roles for rpn11 and ubp6 in deubiquitination and proteolysis by the proteasome. J Biol Chem 2004, 279, 1729-38.
66. Meiners, S. et al. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes. J Biol Chem 2003, 278, 21517-25.
67. Blobel, G. Protein targeting (Nobel lecture). Chembiochem 2000, 1, 86-102.
68. Rechsteiner, M. and Rogers, S. W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 1996, 21, 267-271.
69. Varshavsky, A. The N-end rule: Functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 1996, 93, 12142-12149.
70. Zur, A. and Brandeis, M. Timing of APC/C substrate degradation is determined by fzy/fzr specificity of destruction boxes. Embo J 2002, 21, 4500-10.
71. Orlowski, M. and Wilk, S. Ubiquitinindependent proteolytic functions of the proteasome. Arch Biochem Biophys 2003, 415, 1-5.
72. Grune, T., Merker, K., Sandig, G., and Davies, K. J. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003, 305, 709-18.
73. Peng, J. et al. A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 2003, 21, 921-6.
74. Wu-Baer, F., Lagrazon, K., Yuan, W., and Baer, R. The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J Biol Chem 2003, 278, 34743-6.
75. Spence, J., Sadis, S., Haas, A. L., and Finley, D. A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 1995, 15, 1265-1273.
76. Springael, J. Y., Galan, J. M., Haguenauer-Tsapis, R., and Andre, B. NH4{thorn}-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains. J Cell Sci 1999, 112 (Pt 9), 1375-83.
77. Alberti, S. et al. Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome. J Biol Chem 2002, 277, 45920-7.
78. Chau, V. et al. A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science 1989, 243, 1576-1583.
79. Johnson, E. S., Ma, P. C., Ota, I. M., and Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 1995, 270, 17442-17456.
80. Thrower, J. S., Hoffman, L., Rechsteiner, M., and Pickart, C. M. Recognition of the polyubiquitin proteolytic signal. EMBO J. 2000, 19, 94-102.
81. Young, P., Deveraux, Q., Beal, R., Pickart, C., and Rechsteiner, M. Characterization of two polyubiquitin binding sites in the 26S protease subunit 5a. J. Biol. Chem. 1998, 273, 5461-5467.
82. Hofmann, K. and Falquet, L. A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems. Trends Biochem Sci 2001, 26, 347-50.
83. Swanson, K. A., Kang, R. S., Stamenova, S. D., Hicke, L., and Radhakrishnan, I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. Embo J 2003, 22, 4597-606.
84. Mueller, T. D. and Feigon, J. Structural determinants for the binding of ubiquitin-like domains to the proteasome. Embo J 2003, 22, 4634-45.
85. Ryu, K. S. et al. Binding surface mapping of intra-and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a. J Biol Chem 2003, 278, 36621-7.
86. Hartmann-Petersen, R., Seeger, M., and Gordon, C. Transferring substrates to the 26S proteasome. Trends Biochem Sci 2003, 28, 26-31.
87. Saeki, Y., Saitoh, A., Toh-e, A., and Yokosawa, H. Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis. Biochem Biophys Res Commun 2002, 293, 986-92.
88. Hiyama, H. et al. Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26S proteasome. J Biol Chem 1999, 274, 28019-25.
89. Sakata, E. et al. Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain. EMBO Rep 2003, 4, 301-6.
90. Kleijnen, M. F., Alarcon, R. M., and Howley, P. M. The ubiquitinassociated domain of hPLIC-2 interacts with the proteasome. Mol Biol Cell 2003, 14, 3868-75.
91. Xie, Y. and Varshavsky, A. UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis. Nat Cell Biol 2002, 4, 1003-7.
92. Corn, P. G., McDonald, E. R., 3rd, Herman, J. G., and El-Deiry, W. S. Tat-binding protein-1, a component of the 26S proteasome, contributes to the E3 ubiquitin ligase function of the von Hippel-Lindau protein. Nat Genet 2003, 35, 229-37.
93. Lambertson, D., Chen, L., and Madura, K. Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae. Genetics 1999, 153, 69-79.
94. Murakami, Y. et al. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 1992, 360, 597-9.
95. Sheaff, R. J. et al. Proteasome turnover of p21Cip1 does not require p21Cip1 ubiquitination. Molec. Cell. 2000, 5, 403-410.
96. Zhang, M., Pickart, C. M., and Coffino, P. Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. Embo J 2003, 22, 1488-96.
97. Rezvani, K. et al. Proteasomal interactors control activities as diverse as the cell cycle and glutaminergic neurotransmission. Biochem Soc Trans 2003, 31, 470-3.
98. Touitou, R. et al. A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome. Embo J 2001, 20, 2367-75.
99. Coleman, M. L., Marshall, C. J., and Olson, M. F. Ras promotes p21(Waf1/Cip1) protein stability via a cyclin D1-imposed block in proteasomemediated degradation. Embo J 2003, 22, 2036-46.
100. Murakami, Y., Matsufuji, S., Hayashi, S. I., Tanahashi, N., and Tanaka, K. ATP-Dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation. Mol Cell Biol 1999, 19, 7216-27.
101. Bays, N. W. and Hampton, R. Y. Cdc48-Ufd1-Npl4: stuck in the middle with Ub. Curr Biol 2002, 12, R366-71.
102. Brunger, A. T. and DeLaBarre, B. NSF and p97/VCP: similar at first, different at last. FEBS Lett 2003, 555, 126-33.
103. Rabinovich, E., Kerem, A., Frohlich, K. U., Diamant, N., and Bar-Nun, S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulumassociated protein degradation. Mol Cell Biol 2002, 22, 626-34.
104. Wojcik, C., Yano, M., and DeMartino, G. N. RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasomedependent proteolysis. J Cell Sci 2004, 117, 281-92.
105. Imamura, T. et al. Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome. J Biol Chem 1998, 273, 11183-8.
106. Taxis, C. et al. Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 2003, 278, 35903-13.
107. Tokumoto, T. et al. Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during Xenopus oocyte maturation. BMC Biochem 2003, 4, 6.
108. Gonciarz-Swiatek, M. et al. Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease. J Biol Chem 1999, 274, 13999-4005.
109. Studemann, A. et al. Sequential recognition of two distinct sites in sigma(S) by the proteolytic targeting factor RssB and ClpX. Embo J 2003, 22, 4111-20.
110. Neher, S. B., Sauer, R. T., and Baker, T. A. Distinct peptide signals in the UmuD and UmuD0 subunits of UmuD/D0 mediate tethering and substrate processing by the ClpXP protease. Proc Natl Acad Sci USA 2003, 100, 13219-24.
111. Petroski, M. D. and Deshaies, R. J. Context of multiubiquitin chain attachment influences the rate of Sic1 degradation. Mol Cell 2003, 11, 1435-44.
112. Lee, C., Schwartz, M. P., Prakash, S., Iwakura, M., and Matouschek, A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol Cell 2001, 7, 627-37.
113. Hoskins, J. R., Yanagihara, K., Mizuuchi, K., and Wickner, S. ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence. Proc Natl Acad Sci USA 2002, 99, 11037-42.
114. Lee, C., Prakash, S., and Matouschek, A. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. J Biol Chem 2002, 277, 34760-5.
115. Benaroudj, N., Zwickl, P., Seemuller, E., Baumeister, W., and Goldberg, A. L. ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Mol Cell 2003, 11, 69-78.
116. Kenniston, J. A., Baker, T. A., Fernandez, J. M., and Sauer, R. T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA{thorn} degradation machine. Cell 2003, 114, 511-20.
117. Reid, B. G., Fenton, W. A., Horwich, A. L., and Weber-Ban, E. U. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proc Natl Acad Sci USA 2001, 98, 3768-72.
118. Dillingham, M. S., Wigley, D. B., and Webb, M. R. Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 2000, 39, 205-12.
119. Llorca, O. et al. The 'sequential allosteric ring'mechanism in the eukaryotic chaperonin-assisted folding of actin and tubulin. Embo J 2001, 20, 4065-75.
120. Laskey, R. A. and Madine, M. A. A rotary pumping model for helicase function of MCM proteins at a distance from replication forks. EMBO Rep 2003, 4, 26-30.
121. Flynn, J. M., Neher, S. B., Kim, Y. I., Sauer, R. T., and Baker, T. A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell 2003, 11, 671-83.
122. Palombella, V. J., Rando, O. J., Goldberg, A. L., and Maniatis, T. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 1994, 78, 773-785.
123. Ciechanover, A. et al. Mechanisms of ubiquitin-mediated, limited processing of the NF-kappaB1 precursor protein p105. Biochimie 2001, 83, 341-9.
124. Zhang, M. and Coffino, P. Repeat sequence of Epstein-Barr virus EBNA1 protein interrupts proteasome substrate processing. J Biol Chem 2004, 279, 8635-8641.
125. Hoppe, T. et al. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasomedependent processing. Cell 2000, 102, 577-86.
126. Wojcik, C. and DeMartino, G. N. Analysis of Drosophila 26S proteasome using RNA interference. J Biol Chem 2002, 277, 6188-97.
127. Szlanka, T. et al. Deletion of proteasomal subunit S5a/Rpn10/p54 causes lethality, multiple mitotic defects and overexpression of proteasomal genes in Drosophila melanogaster. J Cell Sci 2003, 116, 1023-33.
128. Mannhaupt, G., Schnall, R., Karpov, V., Vetter, I., and Feldmann, H. Rpn4p acts as a transcription factor by binding to PACE, a nonamer box found upstream of 26S proteasomal and other genes in yeast. FEBS Lett 1999, 450, 27-34.
129. Xie, Y. and Varshavsky, A. RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc Natl Acad Sci USA 2001, 98, 3056-61.
130. Arendt, C. S. and Hochstrasser, M. Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly. Embo J 1999, 18, 3575-85.
131. Nandi, D., Woodward, E., Ginsburg, D. B., and Monaco, J. J. Intermediates in the formation of mouse 20S proteasomes: implications for the assembly of precursor beta subunits. Embo J 1997, 16, 5363-75.
132. Griffin, T. A., Slack, J. P., McCluskey, T. S., Monaco, J. J., and Colbert, R. A. Identification of proteassemblin, a mammalian homologue of the yeast protein, Ump1p, that is required for normal proteasome assembly. Mol Cell Biol Res Commun 2000, 3, 212-7.
133. Ramos, P. C., Hockendorff, J., Johnson, E. S., Varshavsky, A., and Dohmen, R. J. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 1998, 92, 489-99.
134. Santamaria, P. G., Finley, D., Ballesta, J. P., and Remacha, M. Rpn6p, a proteasome subunit from Saccharomyces cerevisiae, is essential for the assembly and activity of the 26S proteasome. J Biol Chem 2003, 278, 6687-95.
135. Yang, Y., Früh, K., Ahn, K., and Peterson, P. A. In vivo assembly of the proteasomal complexes, implications for antigen processing. J. Biol. Chem. 1995, 270, 27687-27694.
136. Mason, G. G., Hendil, K. B., and Rivett, A. J. Phosphorylation of proteasomes in mammalian cells. Identification two phosphorylated subunits and the effect of phosphorylation on activity. Eur. J. Biochem. 1996, 238, 453-462.
137. Mason, G. G., Murray, R. Z., Pappin, D., and Rivett, A. J. Phosphorylation of ATPase subunits of the 26S proteasome. FEBS Lett 1998, 430, 269-74.
138. Kimura, Y. et al. N(alpha)-acetylation and proteolytic activity of the yeast 20 S proteasome. J Biol Chem 2000, 275, 4635-9.
139. Kimura, Y. et al. N-Terminal modifications of the 19S regulatory particle subunits of the yeast proteasome. Arch Biochem Biophys 2003, 409, 341-8.
140. Sumegi, M., Hunyadi-Gulyas, E., Medzihradszky, K. F., and Udvardy, A. 26S proteasome subunits are Olinked N-acetylglucosamine-modified in Drosophila melanogaster. Biochem Biophys Res Commun 2003, 312, 1284-9.
141. Bose, S., Stratford, F. L., Broadfoot, K. I., Mason, G. G., and Rivett, A. J. Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gammainterferon. Biochem J Pt 2004, 378, 177-184.
142. Kurucz, E. et al. Assembly of the Drosophila 26S proteasome is accompanied by extensive subunit rearrangements. Biochem J 2002, 365, 527-36.
143. Tone, Y. and Toh, E. A. Nob1p is required for biogenesis of the 26S proteasome and degraded upon its maturation in Saccharomyces cerevisiae. Genes Dev 2002, 16, 3142-57.
144. Yen, H. C., Gordon, C., and Chang, E. C. Schizosaccharomyces pombe Int6 and Ras homologs regulate cell division and mitotic fidelity via the proteasome. Cell 2003, 112, 207-17.
145. Imai, J., Maruya, M., Yashiroda, H., Yahara, I., and Tanaka, K. The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. Embo J 2003, 22, 3557-67.
146. Bajorek, M., Finley, D., and Glickman, M. H. Proteasome disassembly and downregulation is correlated with viability during stationary phase. Curr Biol 2003, 13, 1140-4.
147. Hendil, K. B., Khan, S. and Tanaka, K. Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes. Biochem. J. 1998, 332, 749-754.
148. Kopp, F., Dahlmann, B., and Kuehn, L. Reconstitution of hybrid proteasomes from purified PA700-20 S complexes and PA28alphabeta activator: ultrastructure and peptidase activities. J Mol Biol 2001, 313, 465-71.
149. Tanahashi, N. et al. Hybrid proteasomes. Induction by interferongamma and contribution to ATPdependent proteolysis. J. Biol. Chem. 2000, 275, 14336-14345.
150. Cascio, P., Call, M., Petre, B., T., W., and Goldberg, A. L. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 2002, 21, 2636-2645.
151. Rechsteiner, M., Realini, C., and Ustrell, V. The proteasome activator 11S REG (PA28) and class I antigen presentation. Biochem. J. 2000, 345, 1-15.
152. Hill, C. P., Masters, E. I., and Whitby, F. G. The 11S regulators of 20S proteasome activity. Curr Top Microbiol Immunol 2002, 268, 73-89.
153. Murata, S. et al. Immunoproteasome assembly and antigen presentation in mice lacking both PA28alpha and PA28beta. Embo J 2001, 20, 5898-907.
154. Murata, S. et al. Growth retardation in mice lacking the proteasome activator PA28gamma. J Biol Chem 1999, 274, 38211-5.
155. Whitby, F. G. et al. Structural basis for the activation of 20 S proteasomes by 11 S regulators. Nature 2000, 408, 115-120.
156. Ustrell, V., Hoffman, L., Pratt, G., and Rechsteiner, M. PA200, a nuclear proteasome activator involved in DNA repair. EMBO J. 2002, 21, 3403-3412.
157. Ho, Y., Gruhler, A., Heilbut, A., Bader, G. D., and Moore, L. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 2002, 415, 180-183.
158. Gavin, A. C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 2002, 415, 141-7.
159. Leggett, D. S. et al. Multiple associated proteins regulate proteasome structure and function. Mol Cell 2002, 10, 495-507.
160. McCutchen-Maloney, S. L. et al. cDNA cloning, expression, and functional characterization of PI31, a proline-rich inhibitor of the proteasome. J Biol Chem 2000, 275, 18557-65.
161. Zaiss, D. M., Standera, S., Kloetzel, P. M., and Sijts, A. J. PI31 is a modulator of proteasome formation and antigen processing. Proc Natl Acad Sci USA 2002, 99, 14344-9.
162. Lu, D. C. et al. A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor. Nat. Medicine 2000, 6, 397-404.
163. Gaczynska, M., Osmulski, P. A., Gao, Y., Post, M. J., and Simons, M. Proline-and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 2003, 42, 8663-70.
164. Yamano, T. et al. Two distinct pathways mediated by PA28 and hsp90 in major histocompatibility complex class I antigen processing. J Exp Med 2002, 196, 185-96.
165. Apcher, G. S. et al. Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits. FEBS Lett 2003, 553, 200-4.
166. Huang, X. et al. The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. J Mol Biol 2002, 323, 771-82.
167. Farout, L. et al. Distribution of proteasomes and of the five proteolytic activities in rat tissues. Arch Biochem Biophys 2000, 374, 207-12.
168. Brooks, P. et al. Subcellular localization of proteasomes and their regulatory complexes in mammalian cells. Biochem. J. 2000, 346, 155-161.
169. Reits, E. A., Benham, A. M., Plougaste, B., Neefjes, J., and Trowsdale, J. Dynamics of proteasome distribution in living cells. EMBO J. 1997, 16, 6087-94.
170. Arabi, A., Rustum, C., Hallberg, E., and Wright, A. P. Accumulation of c-Myc and proteasomes at the nucleoli of cells containing elevated c-Myc protein levels. J Cell Sci 2003, 116, 1707-17.
171. Kopito, R. R. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000, 10, 524-30.
172. Wojcik, C. and DeMartino, G. N. Intracellular localization of proteasomes. Int J Biochem Cell Biol 2003, 35, 579-89.
173. Hampton, R. Y. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 2002, 14, 476-82.
174. McCracken, A. A. and Brodsky, J. L. Evolving questions and paradigm shifts in endoplasmic-reticulumassociated degradation (ERAD). Bioessays 2003, 25, 868-77.