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Conjugation and Deconjugation of Ubiquitin Family Modifiers pp 57–68Cite as

Control of Deneddylation by the COP9 Signalosome

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Part of the book series: Subcellular Biochemistry ((SCBI,volume 54))

Abstract

The interplay between ubiquitin (Ub) family modifiers creates a regulatory network of Ub family proteins which is essential for cell growth and differentiation. One of the best studied crosstalks between Ub family modifiers is the stimulation of ubiquitination by Nedd8 (neural precursor cell expressed developmentally down regulated 8) modification. The neddylation-deneddylation pathway controls the selective ubiquitination of important cellular regulators targeted for proteolysis by the Ub proteasome system (UPS). In this process the cullin scaffolds of cullin-RING Ub ligases (CRLs) are neddylated, which allosterically activates the transfer of Ub to substrates of the CRLs. A major reaction of the regulatory network is the removal of Nedd8 by the COP9 signalosome (CSN), which converts CRLs into an inactive state. The CSN is a conserved protein complex that interacts with CRLs and possesses an intrinsic metalloprotease with a Jab1/Pad1/MPN+ (JAMM) motif responsible for deneddylation.

In the present chapter we focus on the CSN-mediated deneddylation and its biological significance. We summarize latest developments on the mechanism of the CSN and its association with supercomplexes. In addition, data on the regulation of CSN-mediated deneddylation are described. Moreover, dysfunctions of the CSN and their implication in the pathogenesis of diseases are discussed.

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References

  1. Kumar S, Yoshida Y, Noda M. Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem Biophys Res Commun 1993; 195:393–399.

    Article  CAS  PubMed  Google Scholar 

  2. Jentsch S, Pyrowolakis G. Ubiquitin and its kin: how close are the family ties? Trends Cell Biol 2000; 10:335–342.

    Article  CAS  PubMed  Google Scholar 

  3. Liakopoulos D, Doenges G, Matuschewski K et al. A novel protein modification pathway related to the ubiquitin system. EMBO J 1998; 17:2208–2214.

    Article  CAS  PubMed  Google Scholar 

  4. Deng XW, Dubiel W, Wei N et al. Unified nomenclature for the COP9 signalosome and its subunits: an essential regulator of development. Trends Genet 2000; 16:202–203.

    Article  CAS  PubMed  Google Scholar 

  5. Wei N, Deng XW. COP9: a new genetic locus involved in light-regulated development and gene expression in arabidopsis. Plant Cell 1992; 4:1507–1518.

    Article  CAS  PubMed  Google Scholar 

  6. Chamovitz DA, Wei N, Osterlund MT et al. The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch. Cell 1996; 86:115–121.

    Article  CAS  PubMed  Google Scholar 

  7. Wei N, Deng XW. Characterization and purification of the mammalian COP9 complex, a conserved nuclear regulator initially identified as a repressor of photomorphogenesis in higher plants. Photochem Photobiol 1998; 68:237–241.

    Article  CAS  PubMed  Google Scholar 

  8. Seeger M, Kraft R, Ferrell K et al. A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. FASEB J 1998; 12:469–478.

    CAS  PubMed  Google Scholar 

  9. Scheel H, Hofmann K. Prediction of a common structural scaffold for proteasome lid, COP9-signalosome and eIF3 complexes. BMC Bioinformatics 2005; 6:71.

    Article  PubMed  CAS  Google Scholar 

  10. Kapelari B, Bech-Otschir D, Hegerl R et al. Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. J Mol Biol 2000; 300:1169–1178.

    Article  CAS  PubMed  Google Scholar 

  11. Glickman MH, Rubin DM, Coux O et al. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 1998; 94:615–623.

    Article  CAS  PubMed  Google Scholar 

  12. Sharon M, Mao H, Boeri Erba E et al. Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 2009; 17:31–40.

    Article  CAS  PubMed  Google Scholar 

  13. Dohmann EM, Levesque MP, De Veylder L et al. The Arabidopsis COP9 signalosome is essential for G2 phase progression and genomic stability. Development 2008; 135:2013–2022.

    Article  CAS  PubMed  Google Scholar 

  14. Liu C, Powell KA, Mundt K et al. Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and-independent mechanisms. Genes Dev 2003; 17:1130–1140.

    Article  CAS  PubMed  Google Scholar 

  15. Groisman R, Polanowska J, Kuraoka I et al. The ubiquitin ligase activity in the DD B2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 2003; 113:357–367.

    Article  CAS  PubMed  Google Scholar 

  16. Kob R, Kelm J, Posorski N et al. Regulation of the anaphase-promoting complex by the COP9 signalosome. Cell Cycle 2009; 8:2041–2049.

    CAS  PubMed  Google Scholar 

  17. Chamovitz DA. Revisiting the COP9 signalosome as a transcriptional regulator. EMBO Rep 2009; 10:352–358.

    Article  CAS  PubMed  Google Scholar 

  18. Bech-Otschir D, Seeger M, Dubiel W. The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis. J Cell Sci 2002; 115:467–473.

    CAS  PubMed  Google Scholar 

  19. Schweitzer K, Bozko PM, Dubiel W et al. CSN controls NF-kappaB by deubiquitinylation of IkappaBalpha. EMBO J 2007; 26:1532–1541.

    Article  CAS  PubMed  Google Scholar 

  20. Welteke V, Eitelhuber A, Duwel M et al. COP9 signalosome controls the Carma1-Bcl10-Malt1 complex upon T-cell stimulation. EMBO Rep 2009; 10:642–648.

    Article  CAS  PubMed  Google Scholar 

  21. Oren-Giladi P, Krieger O, Edgar BA et al. Cop9 signalosome subunit 8 (CSN8) is essential for Drosophila development. Genes Cells 2008; 13:221–231.

    Article  CAS  PubMed  Google Scholar 

  22. Schwechheimer C. The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim Biophys Acta 2004; 1695:45–54.

    CAS  PubMed  Google Scholar 

  23. Huang X, Langelotz C, Hetfeld-Pechoc BK et al. The COP9 signalosome mediates beta-catenin degradation by deneddylation and blocks adenomatous polyposis coli destruction via USP15. J Mol Biol 2009.

    Google Scholar 

  24. Bech-Otschir D, Kapelari B, Dubiel W. The COP9 signalosome: Its possible role in the ubiquitin system (Mayer JR, Ciechanover A, Rechsteiner M, eds.) Ubiquitin and the Chemistry of Life, Vol. 1, 3 vols. WILEY-VCH Verlag GmbH and KGaA, Weinheim, 2005:348–369.

    Google Scholar 

  25. Neuss H, Huang X, Hetfeld BK et al. The ubiquitin-and proteasome-dependent degradation of COX-2 is regulated by the COP9 signalosome and differentially influenced by coxibs. J Mol Med 2007; 85:961–970.

    Article  CAS  PubMed  Google Scholar 

  26. Pollmann C, Huang X, Mall J et al. The constitutive photomorphogenesis 9 signalosome directs vascular endothelial growth factor production in tumor cells. Cancer Res 2001; 61:8416–8421.

    CAS  PubMed  Google Scholar 

  27. Hetfeld BK, Helfrich A, Kapelari B et al. The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1. Curr Biol 2005; 15:1217–1221.

    Article  CAS  PubMed  Google Scholar 

  28. Zhou C, Wee S, Rhee E et al. Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p. Mol Cell 2003; 11:927–938.

    Article  CAS  PubMed  Google Scholar 

  29. Uhle S, Medalia O, Waldron R et al. Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome. EMBO J 2003; 22:1302–1312.

    Article  CAS  PubMed  Google Scholar 

  30. Huang X, Wagner E, Dumdey R et al. Phosphorylation by COP9 signalosome-associated CK2 promotes degradation of p27 during the G1 cell cycle phase. Isr J Chem 2006; 46:231–238.

    Article  CAS  Google Scholar 

  31. Sun Y, Wilson MP, Majerus PW. Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J Biol Chem 2002; 277:45759–45764.

    Article  CAS  PubMed  Google Scholar 

  32. Cope GA, Suh GS, Aravind L et al. Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8 from Cul1. Science 2002; 298:608–611.

    Article  CAS  PubMed  Google Scholar 

  33. Walden H, Podgorski MS, Huang DT et al. The structure of the APPBP1-UBA3-NED 8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an E1. Mol Cell 2003; 12:1427–1437.

    Article  CAS  PubMed  Google Scholar 

  34. Bohnsack RN, Haas AL. Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer. J Biol Chem 2003; 278:26823–26830.

    Article  CAS  PubMed  Google Scholar 

  35. Gong L, Yeh ET. Identification of the activating and conjugating enzymes of the NED 8 conjugation pathway. J Biol Chem 1999; 274:12036–12042.

    Article  CAS  PubMed  Google Scholar 

  36. Huang DT, Hunt HW, Zhuang M et al. Basis for a ubiquitin-like protein thioester switch toggling E1-E 2 affinity. Nature 2007; 445:394–398.

    Article  CAS  PubMed  Google Scholar 

  37. Pichler A. A second E2 for nedd8ylation expands substrate selection. Structure 2009; 17:321–322.

    Article  CAS  PubMed  Google Scholar 

  38. Kamura T, Conrad MN, Yan Q et al. The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2. Genes Dev 1999; 13:2928–2933.

    Article  CAS  PubMed  Google Scholar 

  39. Morimoto M, Nishida T, Nagayama Y et al. Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability. Biochem Biophys Res Commun 2003; 301:392–398.

    Article  CAS  PubMed  Google Scholar 

  40. Kurz T, Ozlu N, Rudolf F et al. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 2005; 435:1257–1261.

    Article  CAS  PubMed  Google Scholar 

  41. Xirodimas DP, Saville MK, Bourdon JC et al. Mdm2-mediated NED 8 conjugation of p53 inhibits its transcriptional activity. Cell 2004; 118:83–97.

    Article  CAS  PubMed  Google Scholar 

  42. Oved S, Mosesson Y, Zwang Y et al. Conjugation to Nedd8 instigates ubiquitylation and down-regulation of activated receptor tyrosine kinases. J Biol Chem 2006; 281:21640–21651.

    Article  CAS  PubMed  Google Scholar 

  43. Jones J, Wu K, Yang Y et al. A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins. J Proteome Res 2008; 7:1274–1287.

    Article  CAS  PubMed  Google Scholar 

  44. Xirodimas DP, Sundqvist A, Nakamura A et al. Ribosomal proteins are targets for the NED 8 pathway. EMBO Rep 2008; 9:280–286.

    Article  CAS  PubMed  Google Scholar 

  45. Ohki Y, Funatsu N, Konishi N et al. The mechanism of poly-NED 8 chain formation in vitro. Biochem Biophys Res Commun 2009; 381:443–447.

    Article  CAS  PubMed  Google Scholar 

  46. Osaka F, Kawasaki H, Aida N et al. A new NED 8-ligating system for cullin-4A. Genes and Development 1998; 12:2263–2268.

    Article  CAS  PubMed  Google Scholar 

  47. Xirodimas D. Mdm2-Mediated NED 8 Conjugation of p53 Inhibits Its Transcriptional Activity. Cell 2004; 118:83–97.

    Article  CAS  PubMed  Google Scholar 

  48. Rabut G, Peter M. Function and regulation of protein neddylation. ‘Protein modifications: beyond the usual suspects’ review series. EMBO Rep 2008; 9:969–976.

    Article  CAS  PubMed  Google Scholar 

  49. Hori T, Osaka F, Chiba T et al. Covalent modification of all members of human cullin family proteins by NED 8. Oncogene 1999; 18:6829–6834.

    Article  CAS  PubMed  Google Scholar 

  50. Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005; 6:9–20.

    Article  CAS  PubMed  Google Scholar 

  51. Kawakami T, Chiba T, Suzuki T et al. NED 8 recruits E2-ubiquitin to SCF E3 ligase. EMBO J 2001; 20:4003–4012.

    Article  CAS  PubMed  Google Scholar 

  52. Liu J, Furukawa M, Matsumoto T et al. NED 8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Molecular Cell 2002; 10:1511–1518.

    Article  CAS  PubMed  Google Scholar 

  53. Duda DM, Borg LA, Scott DC et al. Structural insights into NED 8 activation of cullin-RING ligases: conformational control of conjugation. Cell 2008; 134:995–1006.

    Article  CAS  PubMed  Google Scholar 

  54. Deshaies RJ, Joazeiro CA. RING domain E3 ubiquitin ligases. Annu Rev Biochem 2009; 78:399–434.

    Article  CAS  PubMed  Google Scholar 

  55. Saha A, Deshaies RJ. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell 2008; 32:21–31.

    Article  CAS  PubMed  Google Scholar 

  56. Morimoto M. Nedd8-modification of Cul1 is promoted by Roc1 as a Nedd8-E 3 ligase and regulates its stability. Biochem Biophys Res Comm 2003; 301:392–398.

    Article  CAS  PubMed  Google Scholar 

  57. Jones J, Wu K, Yang Y et al. A targeted proteomic analysis of the ubiquitin-like modifier nedd8 and associated proteins. J Proteome Res 2008; 7:1274–1287.

    Article  CAS  PubMed  Google Scholar 

  58. Kerscher O, Felberbaum R, Hochstrasser M. Modification of Proteins by Ubiquitin and Ubiquitin-Like Proteins. Annu Rev Cell Dev Biol 2006; 22:159–180.

    Article  CAS  PubMed  Google Scholar 

  59. Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. In Biochim Biophys Acta 2004; 1695:189–207.

    CAS  Google Scholar 

  60. Zhou L, Watts FZ. Nep1, a Schizosaccharomyces pombe deneddylating enzyme. Biochem J 2005; 389:307–314.

    Article  CAS  PubMed  Google Scholar 

  61. Shen LN, Liu H, Dong C et al. Structural basis of NED 8 ubiquitin discrimination by the deNED ylating enzyme NED P1. EMBO J 2005; 24:1341–1351.

    Article  CAS  PubMed  Google Scholar 

  62. Gan-Erdene T. Identification and Characterization of DE N1, a Deneddylase of the ULP Family. Journal of Biological Chemistry 2003; 278:28892–28900.

    Article  CAS  PubMed  Google Scholar 

  63. Wu K, Yamoah K, Dolios Ge et al. DE N1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. J Biol Chem 2003; 278:28882–28891.

    Article  CAS  PubMed  Google Scholar 

  64. Chan Y, Yoon J, Wu J et al. DE N1 deneddylates noncullin proteins in vivo. J Cell Sci 2008; 121:3218–3223.

    Article  CAS  PubMed  Google Scholar 

  65. Gong L, Kamitani T, Millas S et al. Identification of a novel isopeptidase with dual specificity for ubiquitinand NED 8-conjugated proteins. J Biol Chem 2000; 275:14212–14216.

    Article  CAS  PubMed  Google Scholar 

  66. Setsuie R, Wada K. The functions of UCH-L1 and its relation to neurodegenerative diseases. Neurochem Int 2007; 51:105–111.

    Article  CAS  PubMed  Google Scholar 

  67. Choi J, Levey AI, Weintraub ST et al. Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson’s and Alzheimer’s diseases. J Biol Chem 2004; 279:13256–13264.

    Article  CAS  PubMed  Google Scholar 

  68. Ferro A, Carvalho AL, Teixeira-Castro A et al. NED 8: a new ataxin-3 interactor. Biochim Biophys Acta 2007; 1773:1619–1627.

    CAS  PubMed  Google Scholar 

  69. Artavanis-T sakonas K, Misaghi S, Comeaux CA et al. Identification by functional proteomics of a deubiquitinating/deNeddylating enzyme in Plasmodium falciparum. Mol Microbiol 2006; 61:1187–1195.

    Article  CAS  PubMed  Google Scholar 

  70. Schwechheimer C, Serino G, Callis J et al. Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCFTIRI in mediating auxin response. Science 2001; 292:1379–1382.

    Article  CAS  PubMed  Google Scholar 

  71. Lyapina S, Cope G, Shevchenko A et al. Promotion of NED-CUL1 conjugate cleavage by COP9 signalosome. Science 2001; 292:1382–1385.

    Article  CAS  PubMed  Google Scholar 

  72. Panattoni M, Sanvito F, Basso V et al. Targeted inactivation of the COP9 signalosome impairs multiple stages of T-cell development. J Exp Med 2008; 205:465–477.

    Article  CAS  PubMed  Google Scholar 

  73. Wei N, Serino G, Deng XW. The COP9 signalosome: more than a protease. Trends Biochem Sci 2008; 33:592–600.

    Article  CAS  PubMed  Google Scholar 

  74. Wolf DA, Zhou C, Wee S. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Nat Cell Biol 2003; 5:1029–1033.

    Article  CAS  PubMed  Google Scholar 

  75. Cope GA, Deshaies RJ. Targeted silencing of Jab1/Csn5 in human cells downregulates SCF activity through reduction of F-box protein levels. BMC Biochem 2006; 7:1.

    Article  PubMed  CAS  Google Scholar 

  76. Miyauchi Y, Kato M, Tokunaga F et al. The COP9/signalosome increases the efficiency of von Hippel-Lindau protein ubiquitin ligase-mediated hypoxia-inducible factor-alpha ubiquitination. J Biol Chem 2008; 283:16622–16631.

    Article  CAS  PubMed  Google Scholar 

  77. Olma MH, Roy M, Le Bihan T et al. An interaction network of the mammalian COP9 signalosome identifies Dda1 as a core subunit of multiple Cul4-based E3 ligases. J Cell Sci 2009; 122:1035–1044.

    Article  CAS  PubMed  Google Scholar 

  78. Zhou C, Seibert V, Geyer R et al. The fission yeast COP9/signalosome is involved in cullin modification by ubiquitin-related Ned8p. BMC Biochem 2001; 2:7.

    Article  CAS  PubMed  Google Scholar 

  79. Huang X, Hetfeld BK, Seifert U et al. Consequences of COP9 signalosome and 26S proteasome interaction. Febs J 2005; 272:3909–3917.

    Article  CAS  PubMed  Google Scholar 

  80. Peng Z, Shen Y, Feng S et al. Evidence for a physical association of the COP9 signalosome, the proteasome and specific SCF E3 ligases in vivo. Curr Biol 2003; 13:R504–R505.

    Article  CAS  PubMed  Google Scholar 

  81. Maytal-Kivity V, Reis N, Hofmann K et al. MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function. BMC Biochem 2002; 3:28.

    Article  PubMed  Google Scholar 

  82. Berndt C, Bech-Otschir D, Dubiel W et al. Ubiquitin system: JAMMing in the name of the lid. Curr Biol 2002; 12:R815–7.

    Article  CAS  PubMed  Google Scholar 

  83. Yao T, Cohen RE. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature 2002; 419:403–407.

    Article  CAS  PubMed  Google Scholar 

  84. Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 2009; 78:477–513.

    Article  CAS  PubMed  Google Scholar 

  85. Verma R, Aravind L, Oania R et al. Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome. Science 2002; 298:611–615.

    Article  CAS  PubMed  Google Scholar 

  86. Cooper EM, Cutcliffe C, Kristiansen TZ et al. K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1. EMBO J 2009; 28:621–631.

    Article  CAS  PubMed  Google Scholar 

  87. Sato Y, Yoshikawa A, Yamagata A et al. Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains. Nature 2008; 455:358–362.

    Article  CAS  PubMed  Google Scholar 

  88. Hetfeld BK, Peth A, Sun XM et al. The COP9 signalosome-mediated deneddylation is stimulated by caspases during apoptosis. Apoptosis 2008; 13:187–195.

    Article  CAS  PubMed  Google Scholar 

  89. Sun XM, Butterworth M, MacFarlane M et al. Caspase activation inhibits proteasome function during apoptosis. Mol Cell 2004; 14:81–93.

    Article  CAS  PubMed  Google Scholar 

  90. Bornstein G, Ganoth D, Hershko A. Regulation of neddylation and deneddylation of cullin1 in SCFSkp2 ubiquitin ligase by F-box protein and substrate. Proc Natl Acad Sci USA 2006; 103:11515–11520.

    Article  CAS  PubMed  Google Scholar 

  91. Chew EH, Hagen T. Substrate-mediated regulation of cullin neddylation. J Biol Chem 2007; 282:17032–17040.

    Article  CAS  PubMed  Google Scholar 

  92. Tomoda K, Kubota Y, Arata Y et al. The cytoplasmic shuttling and subsequent degradation of p27Kip1 mediated by Jab1/CSN5 and the COP9 signalosome complex. J Biol Chem 2002; 277:2302–2310.

    Article  CAS  PubMed  Google Scholar 

  93. Bech-Otschir D, Kraft R, Huang X et al. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J 2001; 20:1630–1639.

    Article  CAS  PubMed  Google Scholar 

  94. Richardson KS, Zundel W. The emerging role of the COP9 signalosome in cancer. Mol Cancer Res 2005; 3:645–653.

    Article  CAS  PubMed  Google Scholar 

  95. Loda M, Cukor B, Tam SW et al. Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat Med 1997; 3:231–234.

    Article  CAS  PubMed  Google Scholar 

  96. Fullbeck M, Huang X, Dumdey R et al. Novel curcumin-and emodin-related compounds identified by in silico 2D/3D conformer screening induce apoptosis in tumor cells. BMC Cancer 2005; 5:97.

    Article  PubMed  CAS  Google Scholar 

  97. Goel A, Jhurani S, Aggarwal BB. Multi-targeted therapy by curcumin: how spicy is it? Mol Nutr Food Res 2008; 52:1010–1030.

    Article  CAS  PubMed  Google Scholar 

  98. Braumann C, Tangermann J, Jacobi CA et al. Novel anti-angiogenic compounds for application in tumor therapy-COP9 signalosome-associated kinases as possible targets. Mini Rev Med Chem 2008; 8:421–428.

    Article  CAS  PubMed  Google Scholar 

  99. Adler AS, Littlepage LE, Lin M et al. CSN5 isopeptidase activity links COP9 signalosome activation to breast cancer progression. Cancer Res 2008; 68:506–515.

    Article  CAS  PubMed  Google Scholar 

  100. Hsu MC, Huang CC, Chang HC et al. Overexpression of Jab1 in hepatocellular carcinoma and its inhibition by peroxisome proliferator-activated receptor(gamma) ligands in vitro and in vivo. Clin Cancer Res 2008; 14:4045–4052.

    Article  CAS  PubMed  Google Scholar 

  101. Fukumoto A, Ikeda N, Sho M et al. Prognostic significance of localized p27Kip1 and potential role of Jab1/CSN5 in pancreatic cancer. Oncol Rep 2004; 11:277–284.

    CAS  PubMed  Google Scholar 

  102. Kitagawa K, Kotake Y, Kitagawa M. Ubiquitin-mediated control of oncogene and tumor suppressor gene products. Cancer Sci 2009.

    Google Scholar 

  103. Hetfeld BKJ, Bechotschir D, Dubiel W. Purification Method of the COP9 Signalosome from Human Erythrocytes. Meth Enzymol 2005; 398:481–491.

    Article  CAS  PubMed  Google Scholar 

  104. Peth A, Boettcher JP, Dubiel W. Ubiquitin-dependent Proteolysis of the Microtubule End-binding Protein 1, EB1, Is Controlled by the COP9 Signalosome: Possible Consequences for Microtubule Filament Stability. J Mol Biol 2007; 368:550–563.

    Article  CAS  PubMed  Google Scholar 

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  1. Department of General, Visceral, Vascular and Thoracic Surgery, Division of Molecular Biology, Charité, Universitätsmedizin Berlin, Monbijoustrasse 2, 10117, Berlin, Germany

    Tilo Schmaler & Wolfgang Dubiel

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  1. Tilo Schmaler
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  2. Wolfgang Dubiel
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  1. Department of Biology, Division of Immunology, University of Konstanz, Konstanz, Germany

    Marcus Groettrup PhD

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Schmaler, T., Dubiel, W. (2010). Control of Deneddylation by the COP9 Signalosome. In: Groettrup, M. (eds) Conjugation and Deconjugation of Ubiquitin Family Modifiers. Subcellular Biochemistry, vol 54. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6676-6_5

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