The ubiquitin-proteasome pathway and pathogenesis of human diseases

Annual Review of Medicine

Volumn 50, Issue , 1999, Pages 57-74

  Schwartz, Alan L ^a   Ciechanover, Aaron ^b  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b TECHNION ISRAEL INSTITUTE OF TECHNOLOGY   (Israel)

Author keywords

Inflammatory response; Oncoprotein; Protein degradation; Protein turnover; Proteolysis

Indexed keywords

ANTIGEN; CELL SURFACE RECEPTOR; ION CHANNEL; ONCOPROTEIN; PROTEASOME; REGULATOR PROTEIN; UBIQUITIN;

ANTIGEN PRESENTATION; CANCER; CELL CYCLE; CYSTIC FIBROSIS; HAPPY PUPPET SYNDROME; HUMAN; INFLAMMATION; LIDDLE SYNDROME; MUSCLE ATROPHY; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN METABOLISM; REGULATORY MECHANISM; REVIEW; VIRUS INFECTION;

ANTIGEN PRESENTATION; CELL CYCLE; CELL PHYSIOLOGY; DISEASE; GENETIC DISEASES, INBORN; HUMANS; IMMUNE SYSTEM DISEASES; ION CHANNELS; MUSCULAR DISEASES; NEOPLASMS; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEINS; RECEPTORS, CELL SURFACE; UBIQUITINS; VIRUS DISEASES; WASTING SYNDROME;

EID: 0033016291     PISSN: 00664219     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.med.50.1.57     Document Type: Review

References (79)

1. 1. Ciechanover A, Schwartz AL. 1994. Cellular Proteolytic Systems. New York: Wiley
2. 2. Salvesen GS, Dixit VM. 1997. Caspases: intracellular signaling by proteolysis. Cell 91:443-46
3. 3. Ciechanover A, Schwartz AL. 1994. The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins. FASEB 8:182-91
4. 4. Hochstrasser M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405-39
5. 5. Jentsch S, Schlenker S. 1995. Selective protein degradation: a journey's end within the proteasome. Cell 82:881-84
6. 6. Deshaies RJ. 1995. Make it or break it: the role of ubiquitin-dependent proteolysis in cellular regulation. Trends Cell Biol. 5:428-34
7. 7. Ciechanover A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13-21
8. 8. Hershko A, Ciechanover A. 1998. The ubiquitin system. Annu. Rev. Biochem. 67:425-79
9. 9. Rechsteiner M, Hoffman L, Dubiel W. 1993. The multicatalytic and 26S proteasome. J. Biol. Chem. 268:6065-68
10. 10. Peters JM. 1994. Proteasomes: protein degradation machines of the cell. Trends Biochem. Sci. 19:377-82
11. 11. DeMartino GN, Moomaw CR, Zagnitko OP, et al. 1994. PA700, an ATP-dependent activator of the 20S proteasome containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269:20878-84
12. 12. Hoffman L, Rechsteiner M. 1994. Activation of the multicatalytic protease: the 11S regulator and the 20S ATPase complexes contain distinct 30-kilodalton subunits. J. Biol. Chem. 269:16890-95
13. 13. Rock KL, Gramm C, Rothstein L, et al. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761-71
14. 14. Murakami Y, Matsufuji S, Kameji T, et al. 1992. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 380:597-99
15. 15. Stephen AG, Trausch-Azar JS, Ciechanover A, Schwartz AL. 1996. The ubiquitin-activating enzyme E1 is phosphorylated and localized to the nucleus in a cell cycle dependent manner. J. Biol. Chem. 271:15608-14
16. 16. Harbers K, Muller U, Grams A, et al. 1996. Provirus integration into a gene encoding a ubiquitin-conjugating enzyme results in a placental defect and embryonic lethality. Proc. Natl. Acad. Sci. USA 93:12412-17
17. 17. Roest HP, van Klaveren J, deWit J, et al. 1996. Inactivation of the HR6B ubiquitin-conjugating DNA repair enzyme in mice causes male sterility associated with chromatin modification. Cell 86:799-810
18. 18. Reiss Y, Heller H, Hershko A. 1989. Binding sites of ubiquitin-protein ligase. Binding of ubiquitin-protein conjugates and of ubiquitin-carrier protein. J. Biol. Chem. 264:10378-83
19. 19. Dohmen RJ, Madura K, Bartel B, Varshavsky A. 1991. The N-end rule is mediated by the UBC2(RAD6) ubiquitin-conjugating enzyme. Proc. Natl. Acad. Sci. USA 88:7351-55
20. 20. Scheffner M, Huigbretse JM, Howley PM. 1994. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc. Natl. Acad. Sci. USA 91:8797-801
21. 21. Nuber U, Schwarz S, Kaiser P, et al. 1996. Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. J. Biol. Chem. 271:2795-800
22. 22. Kumar S, Kao WH, Howley PM. 1997. Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. J. Biol. Chem. 272:13548-54
23. 23. Gonen H, Schwartz AL, Ciechanover A. 1991. Purification and characterization of a novel protein that is required for the degradation of N-α-acetylated proteins by the ubiquitin system. J. Biol. Chem. 266:19221-31
24. 24. Heller H, Hershko A. 1990. A ubiquitin-protein ligase specific for type 111 protein substrates. J. Biol. Chem. 265:6532-35
25. 25. Scheffner M, Huibregtse JM, Vierstra RD, Howley PM. 1993. The HPV-16 E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495-505
26. 26. Scheffner M, Nuber U, Huigbretse JM. 1995. Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thiolester cascade. Nature 373:81-83
27. 27. Sudakin V, Ganoth D, Dahan A, et al. 1995. The cyclosome, a large complex containing cyclin-selective ubiquitin ligase activity, targets cyclins for destruction at the end of mitosis. Mol. Biol. Cell 6:185-97
28. 28. Irniger S, Piatti S, Michaelis C, Nasmyth K. 1995. Genes involved in sister chromatid separation are needed for B-type cyclin proteolysis in budding yeast. Cell 81:269-77
29. 29. Schneider B, Yang Q, Futcher AB. 1996. Linkage of replication to start by the Cdk inhibitor sic 1. Science 272:560-62
30. 30. Gonen H, Stancovski I, Shkedy D, et al. 1996. Isolation, characterization and partial purification of a novel ubiquitin-protein ligase, E3: targeting of protein substrates via multiple and distinct recognition signals and conjugating enzymes. J. Biol. Chem. 271:302-10
31. 31. Stankovski I, Gonen H, Orian A, et al. 1995. Degradation of the proto-oncogene produces c-Fos by the ubiquitin proteolytic system in vivo and in vitro: identification and characterization of the conjugating enzymes. Mol. Cell Biol. 15:7106-16
32. 32. Orian A, Whiteside S, Israël A, et al. 1995. Ubiquitin-mediated processing of NF-κB transcriptional activator precursor p105: reconstitution of a cell free system and identification of the ubiquitin-carrier protein, E2, and a novel ubiquitin-protein ligase, E3, involved in conjugation. J. Biol. Chem. 270:21707-14
33. 33. Baumiester W, Lupas A. 1997. The proteasome. Curr. Opin. Struct. Biol. 7:273-78
34. 34. Tanaka T, Tsurumi C. 1997. The 26S proteasome: subunits and function. Mol. Biol. Rep. 24:3-11
35. 35. Coux O, Tanaka K, Goldberg AL. 1996. Structure and function of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801-47
36. 36. Larsen CN, Finley D. 1997. Protein translocation channels in the proteasome and other proteases. Cell 91:431-34
37. 37. Lowe J, Stock D, Jap B, et al. 1995. Crystal structure of the 20S proteasome from the archeon, thermoplasma acidophilum. Science 268:533-39
38. 38. Groll M, Ditzel L, Lowe J, et al. 1997. Structure of 20S proteasome from yeast at 2.4Å resolution. Nature 386:463-71
39. 39. Stock D, Nederlof PM, Seemüller E, et al. 1996. Proteasome: from structure to function. Curr. Opin. Biotechnol. 7:376-85
40. 40. Knowlton JR, Johnston SC, Whitby FG, et al. 1997. Structure of the proteasome activator REGα (PA28α). Nature 390:639-43
41. 41. Wilkinson KD, Tashayev VL, O'Connor LB, et al. 1995. Metabolism of the polyubiquitin degradation signal: structure, mechanism and role of isopeptidase T. Biochemistry 34:14535-46
42. 42. Johnston SC, Larsen CN, Cook WJ, et al. 1997. Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 Å resolution. EMBO J. 16:3787-96
43. 43. Hadari T, Warms JVB, Rose IA, Hershko A. 1992. A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation. J. Biol. Chem. 267:719-27
44. 44. Zhu Y, Lambert K, Corless C, et al. 1997. DUB-2 is a member of a novel family of cytokine-inducible deubiquitinating enzymes. J. Biol. Chem. 272:51-57
45. 45. Rogers S, Wells R, Rechsteiner M. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234:364-68
46. 46. Lanker S, Valdivieso MH, Wittenberg C. 1996. Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation. Science 271:1597-600
47. 47. Chen Z, Hagler J, Palombella VJ, et al. 1995. Signal induced site-specific phosphorylation targets IκBα to the ubiquitin-proteasome pathway. Genes Dev. 9:1586-97
48. 48. Musti AM, Treier M, Bohmann D. 1997. Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science 275:400-2
49. 49. Madura K, Varshavsky A. 1994. Degradation of G alpha by the N-end rule pathway. Science 265:1454-58
50. 50. Glotzer M, Murray AW, Kirschner MW. 1991. Cyclin is degraded by the ubiquitin pathway. Nature 349:132-38
51. 51. Hicke L, Riezman H. 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277-87
52. 52. Terrell J, Shih S, Dunn R, Hicke L. 1998. A function for monoubiquitination in the internalization of a G protein-coupled receptor. Mol. Cell. 1:193-202
53. 63 is involved in ubiquitination and endocytosis of a yeast plasma membrane protein. EMBO J. 16:5847-54
54. 54. Kölling R, Hollenberg CP. 1994. The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13:3261-71
55. 55. Galan JM, Moreau V, Andre B, et al. 1996. Ubiquitination mediated by the Npilp/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271:10946-52
56. 56. Kölling R, Losko S. 1997. The linker region of the ABC-transporter Ste6 mediates ubiquitination and fast turnover of the protein. EMBO J. 16:2251-61
57. 57. Strous G, van Kerkhof P, Govers R, et al. 1996. The ubiquitin conjugation system is required for ligand-induced endocytosis and degradation of the growth hormone receptor. EMBO J. 15:3806-12
58. 58. Govers R, van Kerkhof P, Schwartz A, Strous G. 1997. Linkage of the ubiquitin conjugating system and the endocytic pathway in a ligand-induced internalization of the growth hormone receptor. EMBO J. 16:4851-58
59. 59. Scheffner M, Werness BA, Huibregtse JM, et al. 1990. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63:1129-36
60. 60. Treier M, Staszewski LM, Bohmann D. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell 78:787-98
61. 61. Miller JR, Moon RT. 1996. Signal transduction through the β-catenin and specification of cell fate during embryogenesis. Genes Dev. 10:1443-54
62. 62. Aberle H, Bauer A, Stappert J, et al. 1997. β-catenin is a target for ubiquitin-proteasome pathway. EMBO J. 16:3797-804
63. 63. Ward CL, Omura S, Kopito RR. 1995. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83:121-27
64. 64. Jensen TJ, Loo MA, Pind S, et al. 1995. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83:129-35
65. 65. Kishino T, Lalande M, Wagstaff J. 1997. UBE3A/E6-AP mutations cause Angelman syndrome. Nat. Genet. 15:70-73
66. 66. Sutcliffe JS, Jiang YH, Galijaard RJ, et al. 1997. The E6-Ap ubiquitin-protein ligase (UBE3A) gene is localized within a narrowed Angelman syndrome critical region. Genome Res. 7:368-77
67. 67. Albrecht U, Sutcliffe JS, Cattanach BM, et al. 1997. Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons. Nat. Genet. 17:75-78
68. 68. Staub O, Dho S, Henry P, et al. 1996. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J. 15:2371-80
69. 69. Staub O, Gautschi I, Ishikawa T, et al. 1997. Regulation of stability and function of the epithelial Na+ channel (EnaC) by ubiquitination. EMBO J. 16:6325-36
70. 70. May MJ, Ghosh S. 1998. Signal transduction through NF-kB. Immunol. Today 19:80-88
71. 71. Levitskaya J, Sharipo A, Leonchiks A, et al. 1997. Inhibition of ubiquitin-proteasome-dependent protein degradation by the Gly-A1a repeat domain of the Epstein-Barr Virus Nuclear Antigen (EBNA)-1. Proc. Natl. Acad. Sci. USA 94:12616-21
72. 72. Wiertz EJ, Tortorella D, Bogyo M, et al. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 84:432-38
73. 73. van Leeuwen FW, de Kleijn DPV, van den Hurk HH, et al. 1998. Frameshift mutants of β-amyloid precursor protein and ubiquitin-B in Alzheimer's and Downs patients. Science 279:242-47
74. 74. Mitch WE, Goldberg AL. 1996. Mechanisms of muscle wasting: the role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335:1897-1905
75. 75. Tiao G, Fagan JM, Samuels N, et al. 1994. Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94:2255-64
76. 2+-activated, and ubiquitin-proteasome proteolytic pathways. J. Clin. Invest. 97:1610-17
77. 77. Tiao G, Hobler S, Wang JJ, et al. 1997. Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. J. Clin. Invest. 99:163-68
78. 78. Tawa NE Jr, Odessey R, Goldberg AL. 1997. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J. Clin. Invest. 100:197-203
79. 79. Perry WL, Hustad CM, Swing DA, et al. 1998. The itchy locus encodes a novel ubiquitin protein ligase that is disrupted in a18H mice. Nat. Genet. 18:143-46