The COP9 signalosome (CSN): An evolutionary conserved proteolysis regulator in eukaryotic development

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1695, Issue 1-3, 2004, Pages 45-54

  Schwechheimer, Claus ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

26S proteasome; COP9 signalosome; Development; E3 ubiquitin ligase; Proteolysis; Ubiquitin

Indexed keywords

COP9 SIGNALOSOME; PEPTIDASE; PROTEASOME; PROTEIN; PROTEIN KINASE; PROTEIN SUBUNIT; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

CAENORHABDITIS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DROSOPHILA; ENZYME ACTIVITY; EUKARYOTE EVOLUTION; FUNGUS; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN; PHOTOMORPHOGENESIS; PLANT DEVELOPMENT; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; UBIQUITINATION; YEAST;

ANIMALS; ARABIDOPSIS; ARABIDOPSIS PROTEINS; MAMMALS; MULTIPROTEIN COMPLEXES; PEPTIDE HYDROLASES; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN KINASES; PROTEINS; SIGNAL TRANSDUCTION; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; YEASTS;

ARABIDOPSIS; EUKARYOTA;

EID: 9644272422     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.09.023     Document Type: Review

References (98)

1. N. Wei, and X.-W. Deng COP9: a new genetic locus involved in light-regulated development and gene expression in Arabidopsis Plant Cell 4 1992 1507 1518
2. S.F. Kwok, B. Piekos, S. Miséra, and X.-W. Deng A complement of ten essential and pleiotropic Arabidopsis COP/DET/FUS genes is necessary for repression of photomorphogenesis in darkness Plant Physiol. 110 1996 731 742
3. N. Wei, D.A. Chamovitz, and X.-W. Deng Arabidopsis COP9 is a component of a novel signaling complex mediating light control of development Cell 78 1994 117 124
4. D.A. Chamovitz, N. Wei, M.T. Osterlund, A.G. von Arnim, J.M. Staub, M. Matsui, and X.-W. Deng The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch Cell 86 1996 115 121
5. J.M. Staub, N. Wei, and X.-W. Deng Evidence for FUS6 as a component of the nuclear-localized COP9 complex in Arabidopsis Plant Cell 8 1996 2047 2056
6. G. Serino, T. Tsuge, S. Kwok, M. Matsui, N. Wei, and X.-W. Deng Arabidopsis cop8 and fus4 mutations define the same gene that encodes subunit 4 of the COP9 signalosome Plant Cell 11 1999 1967 1979
7. B. Karniol, P. Malec, and D.A. Chamovitz Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of the COP9 complex Plant Cell 11 1999 839 848
8. Z. Peng, G. Serino, and X.-W. Deng A role of Arabidopsis COP9 signalosome in multifaceted developmental processes revealed by the characterization of its subunit 3 Development 128 2001 4277 4288
9. G. Serino, H. Su, Z. Peng, T. Tsuge, N. Wei, H. Gu, and X.W. Deng Characterization of the last subunit of the Arabidopsis COP9 signalosome: implications for the overall structure and origin of the complex Plant Cell 15 2003 719 731
10. M. Seeger, R. Kraft, K. Ferrell, D. Bech-Otschir, R. Dumdy, R. Schade, C. Gordon, M. Naumann, and W. Dubiel A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits FASEB J. 12 1998 469 478
11. N. Wei, T. Tsuge, G. Serino, N. Dohmae, K. Takio, and X.-W. Deng The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex Curr. Biol. 8 1998 919 922
12. N. Wei, and X.-W. Deng Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants Photomorph. Photobiol. 68 2 1998 237 241
13. S. Freilich, E. Oron, Y. Kapp, Y. Nevo-Caspi, S. Orgad, D. Segal, and D.A. Chamovitz The COP9 signalosome is essential for development of Drosophila melanogaster Curr. Biol. 9 1999 1187 1190
14. K.E. Mundt, J. Porte, J.M. Murray, C. Brikos, P. Christensen, T. Caspari, I.M. Hagan, J.B.A. Millar, V. Simanis, K. Hofmann, and A.M. Carr The COP9/signalosome complex is conserved in fission yeast and has a role in S phase Curr. Biol. 9 1999 1427 1430
15. L. Pintard, T. Kurz, S. Glaser, J.H. Willis, M. Peter, and B. Bowerman Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin for degradation at the meiosis-to-mitosis transition in C. elegans Curr. Biol. 13 2003 911 921
16. S. Busch, S.E. Eckert, S. Krappmann, and G.H. Braus The COP9 signalosome is an essential regulator of development in the filamentous fungus Aspergillus nidulans Mol. Microbiol. 49 2003 717 730
17. S. Wee, B. Hetfeld, W. Dubiel, and D.A. Wolf Conservation of the COP9/Signalosome in budding yeast BMC Genetics 3 2002 15
18. V. Maytal-Kivity, R. Piran, E. Pick, K. Hofmann, and M.H. Glickman COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae EMBO Rep. 13 2002 1215 1221
19. X.-W. Deng, W. Dubiel, N. Wei, K. Hofmann, K. Mundt, J. Colicelli, J.-Y. Kato, M. Naumann, D. Segal, M. Seeger, M. Glickman, and D.A. Chamovitz Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development Trends Genet. 16 2000 202 203
20. W. Baumeister, J. Walz, F. Zühl, and E. Seemüller The proteasome: paradigm of a self-compartmentalizing protease Cell 92 1998 367 380
21. M.H. Glickman, D.M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V.A. Fried, and D. Finley A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3 Cell 94 1998 615 623
22. L. Aravind, and C.P. Ponting Homologues of the 26S proteasome are regulators of transcription and translation Protein Sci. 7 1998 1250 1254
23. K. Hofmann, and P. Bucher The PCI domain: a common theme in three multiprotein complexes Trends Biochem. Sci. 23 1998 204 205
24. K.S. Browning, D.R. Gallie, J.W.B. Hershey, A.G. Hinnebusch, U. Maitra, W.C. Merrick, and C. Norbury Unified nomenclature of eukaryotic initiation factor 3 Trends Biochem. Sci. 26 2001 284
25. H. Fu, N. Reis, Y. Lee, M.H. Glickman, and R.D. Vierstra Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome EMBO J. 20 2001 7096 7107
26. T.-H. Kim, K. Hofmann, A.G. von Arnim, and D.A. Chamovitz PCI complexes: pretty complex interactions in diverse signaling pathways Trends Plant Sci. 6 2001 379 386
27. G.A. Cope, G.S.B. Suh, L. Aravind, S.E. Schwarz, S.L. Zipursky, E.V. Koonin, and R.J. Deshaies Role for predicted metalloprotease motif of JAB1/Csn5 in cleavage of NEDD8 from CUL1 Science 298 2002 608 611
28. R. Verma, L. Aravind, R. Oania, W.H. McDonald, J.R. Yates, E.V. Koonin, and R.J. Deshaies Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome Science 298 2002 611 615
29. A. Hershko, and A. Chiechanover The ubiquitin system Annu. Rev. Biochem. 67 1998 425 479
30. R.J. Deshaies SCF and Cullin/RING H2-based ubiquitin ligases Annu. Rev. Cell Dev. Biol. 15 1999 435 467
31. S. Lyapina, G. Cope, A. Shevchenko, G. Serino, C. Zhou, D.A. Wolf, N. Wei, A. Shevchenko, and R.J. Deshaies COP9 Signalosome promotes cleavage of NEDD8-CUL1 conjugates Science 292 2001 1382 1385
32. TIR1 in mediating auxin response Science 292 2001 1379 1382
33. C. Schwechheimer, G. Serino, and X.-W. Deng Multiple ubiquitin-ligase- mediated processes require COP9 signalosome and AXR1 function Plant Cell 14 2002 2553 2563
34. I.E. Wertz, K.M. O'Rourke, Z. Zhang, D. Dornan, D. Arnott, R.J. Deshaies, and V.M. Dixit Human de-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase Science 303 2004 1371 1374
35. C. Zhou, V. Seibert, R. Geyer, E. Rhee, S. Lyapina, G. Cope, R.J. Deshaies, and D.A. Wolf The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p BMC Biochem. 2 2001 7
36. X. Yang, S. Menon, K. Lykke-Andersen, T. Tsuge, D. Xiao, X. Wang, R.J. Rodriguez-Suarez, H. Zhang, and N. Wei The COP9 signalosome inhibits p27kip1 degradation and impedes G1-S phase progression via deneddylation of SCF Cul1 Curr. Biol. 12 2002 667 672
37. M.-K. Bae, M.-Y. Ahn, J.-W. Jeong, M.-H. Bae, Y.-M. Lee, S.-K. Bae, J.-W. Park, K.-R. Kim, and K.-W. Kim JAB1 interacts directly with HIF-1α and regulates its stability J. Biol. Chem. 277 2002 9 12
38. R. Groisman, J. Polanowska, I. Kuraoka, J.-I. Sawada, M. Siaijo, K. Tanaka, and Y. Nakatani The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage Cell 113 2003 357 367
39. C. Liu, K.A. Powell, K. Mundt, L. Wu, A.M. Carr, and T. Caspari Cop9/signalosome subunits and Pcu4 regulate ribonucletide reductase by boh checkpoint-dependent and-independent mechanisms Genes Dev. 17 2003 1130 1140
40. L.A.A. Higa, I.S. Mihaylov, D.P. Banks, J. Zhneg, and H. Zhang Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint Nat. Cell Biol. 5 2003 1008 1015
41. F. Osaka, M. Saeki, S. Katayama, N. Aida, A. Toh-e, K. Kominami, T. Toda, T. Suzuki, T. Chiba, K. Tanaka, and S. Kato Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission yeast EMBO J. 19 2000 3475 3484
42. T. Hori, F. Osaka, T. Chiba, C. Miyamoto, K. Okabayashi, N. Shimbara, S. Kato, and K. Tanaka Covalent modification of all members of human cullin family proteins by NEDD8 Oncogene 18 1999 6829 6834
43. V. Maytal-Kivity, N. Reis, K. Hofmann, and M.H. Glickman MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function BMC Biochem. 3 2002 28
44. H.J.T.T. Tran, M.D. Allen, J. Löwe, and M. Bycroft Structure of the Jab1/MPN domain and its implications for proteasome function Biochemistry 42 2003 11460 11465
45. X.I. Ambroggio, D.C. Rees, and R.J. Deshaies JAMM: a metalloprotease-like zinc site in the proteasome and signalosome PLoS Biol. 2 2004 0113 0119
46. J. Zheng, X. Yang, J.M. Harrell, S. Ryzhikov, E.-H. Shim, K. Lykke-Andersen, N. Wei, H. Sun, R. Kobayashi, and H. Zhang CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex Mol. Cell 10 2002 1519 1526
47. Cand1, an inhibitor of CUL1-SKP1 binding and SCF ligases Mol. Cell 10 2002 1511 1518
48. Y. Cheng, X. Dai, and Y. Zhao AtCAND1, a HEAT-repeat protein that participates in auxin signaling in Arabidopsis Plant Phys. 135 2004 1020 1026
49. D. Bech-Otschir, R. Kraft, X. Hunag, P. Henklein, B. Kapelari, C. Pollmann, and W. Dubiel COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system EMBO J. 20 2001 1630 1639
50. D. Dornan, I. Wertz, H. Shimizu, D. Arnott, G.D. Frantz, P. Dowd, K.M. O'Rourke, H. Koeppen, and V.M. Dixit The ubiquitin ligase COP1 is a critical negative regulator of p53 Nature 429 2004 86 92
51. Y. Sun, M.P. Wilson, and P.W. Majerus Inositol 1.3.4-triphosphate 5/6-kinase associates with the COP9 signalosome J. Biol. Chem. 277 2002 31857 31862
52. M.P. Wilson, Y. Sun, L. Chao, and P.W. Majerus Inositol 1,3,4-triphosphate 5/6 kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2 J. Biol. Chem. 276 2001 40998 41004
53. S. Uhle, O. Medalia, R. Waldron, R. Dumdey, P. Henklein, D. Bech-Otschir, X. Huang, M. Berse, J. Sperling, R. Schade, and W. Dubiel Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome EMBO J. 22 2003 1302 1312
54. C. Zhou, S. Wee, E. Rhee, M. Naumann, W. Dubiel, and D.A. Wolf Fission yeast COP9/Signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p Mol. Cell 11 2003 927 938
55. Z. Peng, G. Serino, and X.-W. Deng Molecular characterization of subunit 6 of the COP9 signalosome and its role in multifaceted development processes in Arabidopsis Plant Cell 13 2001 2393 2407
56. C. Schwechheimer, and P. Dodds A breakdown in defense signalling Plant Cell 14 2002 S5 S8
57. X. Wang, S. Feng, N. Nakayama, W.L. Crosby, V.F. Irish, X.W. Deng, and N. Wei The COP9 Signalosome interacts with SCFUFO and participates in Arabidopsis flower development Plant Cell 15 2003 1071 1082
58. COI1 and modulates jasmonate responses Plant Cell 15 2003 1083 1094
59. X.-W. Deng, M. Matsui, N. Wei, D. Wagner, A.M. Chu, K.A. Feldmann, and P.H. Quail COP1, an Arabidopsis regulatory gene encodes a protein with both a zinc-binding motif and a Gβ homologous domain Cell 71 1992 791 801
60. A. Pepper, T. Delaney, T. Wahsburn, D. Poole, and J. Chory DET1, a negative regulator of light-mediated development and gene expression in Arabidopsis, encodes a novel nuclear-localized protein Cell 78 1994 109 116
61. M. Holm, L. Ma, L.-J. Qu, and X.-W. Deng Two interacting bZIP proteins are direct targets of COP1-mediated control of light-dependent gene expression in Arabidopsis Genes Dev. 16 2002 1247 1259
62. H.S. Seo, E. Watanabe, S. Tokutomi, A. Nagatani, and N.-H. Chua Photoreceptor ubiquitination by COP1 E3 ligase desensitizes phytochrome A signaling Genes Dev. 18 2004 617 622
63. H.S. Seo, J.-Y. Yang, M. Ishikawa, C. Bolle, M.L. Ballesteros, and N.-H. Chua LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated by SPA1 Nature 423 2003 995 999
64. H. Wang, L. Ma, J.-M. Li, H.-Y. Zhao, and X.W. Deng Direct interaction of Arabidopsis cryptochromes with COP1 in light control development Science 294 2001 154 159
65. M.T. Osterlund, C.S. Hardtke, N. Wei, and X.-W. Deng Targeted destabilization of HY5 during light-regulated development of Arabidopsis Nature 405 2000 462 466
66. Y. Saijo, J.A. Sullivan, H. Wang, J.-Y. Yang, Y. Shen, V. Rubia, L. Ma, U. Hoecker, and X.W. Deng The COP1-SPA1 interaction defines a critical step in phytochrome A-mediated regulation of HY5 activity Genes Dev. 17 2003 3642 3647
67. M.T. Osterlund, L.-H. Ang, and X.-W. Deng The role of COP1 in repression of Arabidopsis photomorphogenic development Trends Cell Biol. 9 1999 113 118
68. M. Muratani, and W.P. Tansey How the ubiquitin-proteasome system controls transcription Nat. Rev., Mol. Cell Biol. 4 2003 1 10
69. G.S. Suh, B. Poeck, T. Chouard, E. Oron, D. Segal, D.A. Chamovitz, and S.L. Zipursky Drosophila JAB1/CSN5 acts in photoreceptor cells to induce glial cells Neuron 33 2002 35 46
70. E. Oron, M. Mannervik, S. Rencus, O. Harari-Steinberg, S. Neumann-Silberberg, D. Segal, and D. Chamovitz COP9 signalosome subunits 4 and 5 regulate multiple pleiotropic pathways in Drosophila melanogaster Development 129 2002 4399 4409
71. S. Doronkin, I. Djagaeva, and S.K. Beckendorf The COP9 signalosome promotes degradation of cyclin E during early Drosophila oogenesis Dev. Cell 4 2003 699 710
72. P. Smith, W.-M. Leung-Chiu, R. Montgomery, A. Orsborn, K. Kuznicki, E. Gressman-Colberly, L. Mutapic, and K. Bennett The GLH proteins, Caenorhabditis elegans P granule components, associate with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a predicted cytoskeletal protein Dev. Biol. 251 2002 333 347
73. J. Yan, K. Walz, H. Nakamura, S. Carattini-Rivera, Q. Zhao, H. Vogel, N. Wei, M.J. Justice, A. Bradley, and J.R. Lupski COP9 signalosome subunit 3 is essential for maintenance of cell proliferation in the mouse embryonic epiblast Mol. Cell. Biol. 23 2003 6798 6808
74. K. Lykke-Andersen, L. Schaefer, S. Menon, X.-W. Deng, J.B. Miller, and N. Wei Disruption of the COP9 signalosome CSN2 subunit in mice causes deficient cell proliferation, accumulationn of p53 and cyclin E, and early embryonc death Mol. Cell. Biol. 23 2003 6790 6797
75. F.-X. Claret, M. Hibi, S. Dhut, T. Toda, and M. Karin A new group of conserved coactivators that increase the specificity of AP-1 transcription factors Nature 383 1996 453 457
76. T. Tsuge, M. Matsui, and N. Wei The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain J. Mol. Biol. 305 2001 1 9
77. R. Kleemann, A. Hausser, G. Geiger, R. Mischke, A. Burger-Kentischer, O. Flieger, F.-J. Johannes, T. Roger, T. Calandra, A. Kapurniotu, M. Grell, D. Finkelmeier, H. Brunner, and J. Bernhagen Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1 Nature 408 2000 211 216
78. M. Naumann, D. Bech-Otschir, Z. Huang, K. Ferrell, and W. Dubiel COP9 signalosome-directed c-JUN activation/stabilization is independent of JNK J. Biol. Chem. 274 1999 32768
79. E. Bianchi, S. Denti, A. Granata, G. Bossi, J. Geginat, A. Villa, L. Rogge, and R. Pardl Integrin LFA-1 interacts with the transcriptional co-acitvator JAB1 to modulate AP1 activity Nature 404 2000 617 621
80. V.A. Boussiotis, G.J. Freeman, P.A. Taylor, A. Berezovskaya, I. Grass, B.R. Blazar, and L.M. Nadler p27Kip1 funcions as an anergy factor inhibiting interleukin 2 transcription and clonal expansion of alloreactive human and mouse helper T lymphocytes Nat. Med. 6 2000 290 297
81. Kip1 is instigated by JAB1 Nature 398 1999 160 165
82. K. Tomoda, Y. Kubota, Y. Arata, S. Mori, M. Maeda, T. Tanaka, M. Yoshida, N. Yoneda-Kato, and J.-Y. Kato The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex J. Biol. Chem. 277 2002 2302 2310
83. K.E. Mundt, C. Liu, and A.M. Carr Deletion mutants in COP9/signalosome subunits in fission yeast Schizosaccharomyces pombe display distinct phenotypes Mol. Biol. Cell 13 2002 493 502
84. T. Bondar, A. Ponomarev, and P. Raychaudhuri Ddb1 is required for the proteolysis of the Schizosaccharomyces pombe replication inhibitor Spd1 during S phase and after DNA damage J. Biol. Chem. 279 2004 9937 9943
85. R. Dechend, F. Hirano, K. Lehmann, V. Heissmeyer, S. Ansieau, F.G. Wulczyn, C. Scheidereit, and A. Leutz The Bcl-3 oncoprotein acts as a bridging factor between NF-κB/Rel and nuclear co-regulators Oncogene 18 1999 3316 3323
86. S. Müller, M. Berger, F. Lehembre, J.-S. Seeler, Y. Haupt, and A. Dejean c-Jun and p53 activity is modulated by SUMO-1 modification J. Biol. Chem. 275 2000 13321 13329
87. M.-L. Hermida-Matsumoto, P.B Chock, T. Curran, and D.C.H Yang Ubiquitinylation of transcription factors c-Jun and c-Fos using reconstituted ubiquitinylation enzymes J. Biol. Chem. 271 1996 4930 4936
88. M.A. Boumpheng, J.J. Dimas, S.G. Dodds, and B.A. Christy Degradation of Id proteins by the ubiquitin-proteasome pathway FASEB J. 13 2000 2257 2264
89. H. Cohen, A. Azriel, T. Cohen, D. Meraro, S. Hashmueli, D. Bech-Otschir, R. Kraft, W. Dubiel, and B.-Z. Levi Interaction between interferon consensus sequence-binding protein and COP9/signalosome subunit CSN2 (TRIP15) J. Biol. Chem. 275 2000 39081 39089
90. J. Roth, M. Dobbelstein, D.A. Freedman, T. Shenk, and A.J. Levine Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein EMBO J. 17 1998 554 564
91. A. Chauchereau, M. Georgiakaki, M. Perrin-Wolff, E. Milgrom, and H. Loosfelt JAB1 interacts with both the progesterone receptor and SRC-1 J. Biol. Chem. 275 2000 8540 8548
92. H. Poulla, U. Karvonen, O.A. Jänne, and J.J. Palvimo Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1) Proc. Natl. Acad. Sci. 97 2000 14145 14150
93. E. Kopf, J.-L. Plassat, V. Vivat, H. de Thé, P. Chambon, and C. Rochette-Egly Dimerization with retinoic X receptors and phosphorylation modulate the retinoic acid-induced degradation of retinoic acid receptors α and γ through the ubiquitin-proteasome pathway J. Biol. Chem. 275 2000 33280 33288
94. J.D. Chen, and R.M. Evans A transcriptional co-repressor that interacts with nuclear hormone receptors Nature 377 1995 454 457
95. A. Dace, L. Zhao, K.S. Park, T. Furuno, M. Nakanishi, B. West, J.A. Hanover, and S.-Y. Cheng Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptor Proc. Natl. Acad. Sci. 97 2000 8985 8990
96. SKP2 Curr. Biol. 11 2001 263 267
97. S. Li, X. Liu, and M. Ascoli p38JAB1 binds to the intracelleular precursor of the lutropin/choriogonadotropin receptor and promotes its degradation J. Biol. Chem. 275 2000 13386 13393
98. S. Mahalingam, V. Ayyavoo, M. Patel, T. Kieber-Emmons, G.D. Kao, R.J. Muschel, and D.B. Weiner HIV-1 Vpr interacts with a human 34-kDa mov34 homologue, a cellular factor linked to the G2/M phase transition of the mammalian cell cycle Proc. Natl. Acad. Sci. 95 1998 3419 3424