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Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms

de Bie, P, Ciechanover, A·2011·Cell Death & Differentiation

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  1. Kee Y, Huibregtse JM . Regulation of catalytic activities of HECT ubiquitin ligases. Biochem Biophys Res Commun 2007; 354: 329–333. · DOI
  2. Levkowitz G, Waterman H, Ettenberg SA, Katz M, Tsygankov AY, Alroy I et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-CBL/SLI-1. Mol Cell 1999; 4: 1029–1040. · DOI
  3. Vodermaier HC . APC/C and SCF: controlling each other and the cell cycle. Curr Biol 2004; 14: R787–R796. · DOI
  4. Debonneville C, Flores SY, Kamynina E, Plant PJ, Tauxe C, Thomas MA et al. Phosphorylation of NEDD4-2 by SGK1 regulates epithelial Na(+) channel cell surface expression. EMBO J 2001; 20: 7052–7059. · DOI · Paper page
  5. Ben-Saadon R, Zaaroor D, Ziv T, Ciechanover A . The polycomb protein RING1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity. Mol Cell 2006; 24: 701–711. · DOI
  6. Cao R, Tsukada Y, Zhang Y . Role of BMI-1 and RING1A in H2A ubiquitylation and Hox gene silencing. Mol Cell 2005; 20: 845–854. · DOI
  7. Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA . Structural insights into NEDD8 activation of Cullin-RING ligases: conformational control of conjugation. Cell 2008; 134: 995–1006. · DOI · Paper page
  8. Saha A, Deshaies RJ . Multimodal activation of the ubiquitin ligase SCF by NEDD8 conjugation. Mol Cell 2008; 32: 21–31. · DOI
  9. Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM . RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc Natl Acad Sci USA 1999; 96: 11364–11369. · DOI
  10. Huibregtse JM, Scheffner M, Beaudenon S, Howley PM . A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc Natl Acad Sci USA 1995; 92: 2563–2567. · DOI
  11. Nuber U, Schwarz SE, Scheffner M . The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate. Eur J Biochem 1998; 254: 643–649. · DOI · Paper page
  12. Hu G, Fearon ER . SIAH-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. Mol Cell Biol 1999; 19: 724–732. · DOI
  13. Yin Q, Lin SC, Lamothe B, Lu M, Lo YC, Hura G et al. E2 interaction and dimerization in the crystal structure of TRAF6. Nat Struct Mol Biol 2009; 16: 658–666. · DOI
  14. Galan JM, Peter M . Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc Natl Acad Sci USA 1999; 96: 9124–9129. · DOI
  15. Gallagher E, Gao M, Liu YC, Karin M . Activation of the E3 ubiquitin ligase Itch through a phosphorylation-induced conformational change. Proc Natl Acad Sci USA 2006; 103: 1717–1722. · DOI · Paper page
  16. Bruce MC, Kanelis V, Fouladkou F, Debonneville A, Staub O, Rotin D . Regulation of NEDD4-2 self-ubiquitination and stability by a PY motif located within its HECT-domain. Biochem J 2008; 415: 155–163. · DOI
  17. Wiesner S, Ogunjimi AA, Wang HR, Rotin D, Sicheri F, Wrana JL et al. Autoinhibition of the HECT-type ubiquitin ligase SMURF2 through its C2 domain. Cell 2007; 130: 651–662. · DOI
  18. Fang S, Jensen JP, Ludwig RL, Vousden KH, Weissman AM . Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 2000; 275: 8945–8951. · DOI · Paper page
  19. Kao WH, Beaudenon SL, Talis AL, Huibregtse JM, Howley PM . Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase. J Virol 2000; 74: 6408–6417. · DOI
  20. Ryan PE, Davies GC, Nau MM, Lipkowitz S . Regulating the regulator: negative regulation of CBL ubiquitin ligases. Trends Biochem Sci 2006; 31: 79–88. · DOI
  21. Petroski MD, Deshaies RJ . Function and regulation of Cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005; 6: 9–20. · DOI · Paper page
  22. Coutts AS, Adams CJ, La Thangue NB . p53 ubiquitination by Mdm2: a never ending tail? DNA Repair (Amst) 2009; 8: 483–490. · DOI
  23. Itahana K, Mao H, Jin A, Itahana Y, Clegg HV, Lindstrom MS et al. Targeted inactivation of Mdm2 RING finger E3 ubiquitin ligase activity in the mouse reveals mechanistic insights into p53 regulation. Cancer Cell 2007; 12: 355–366. · DOI · Paper page
  24. Linares LK, Kiernan R, Triboulet R, Chable-Bessia C, Latreille D, Cuvier O et al. Intrinsic ubiquitination activity of PCAF controls the stability of the oncoprotein HDM2. Nat Cell Biol 2007; 9: 331–338. · DOI
  25. Ettenberg SA, Magnifico A, Cuello M, Nau MM, Rubinstein YR, Yarden Y et al. CBL-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex. J Biol Chem 2001; 276: 27677–27684. · DOI
  26. Zeng S, Xu Z, Lipkowitz S, Longley JB . Regulation of stem cell factor receptor signaling by CBL family proteins (CBL-b/c-CBL). Blood 2005; 105: 226–232. · DOI
  27. Alwan HA, van Zoelen EJ, van Leeuwen JE . Ligand-induced lysosomal epidermal growth factor receptor (EGFR) degradation is preceded by proteasome-dependent EGFR de-ubiquitination. J Biol Chem 2003; 278: 35781–35790. · DOI
  28. Wang Y, Yeung YG, Langdon WY, Stanley ER . c-CBL is transiently tyrosine-phosphorylated, ubiquitinated, and membrane-targeted following CSF-1 stimulation of macrophages. J Biol Chem 1996; 271: 17–20. · DOI
  29. Schmidt MH, Hoeller D, Yu J, Furnari FB, Cavenee WK, Dikic I et al. ALIX/AIP1 antagonizes epidermal growth factor receptor downregulation by the CBL-SETA/CIN85 complex. Mol Cell Biol 2004; 24: 8981–8993. · DOI
  30. Lennartsson J, Wardega P, Engstrom U, Hellman U, Heldin CH . ALIX facilitates the interaction between c-CBL and platelet-derived growth factor beta-receptor and thereby modulates receptor down-regulation. J Biol Chem 2006; 281: 39152–39158. · DOI
  31. Li Y, Gazdoiu S, Pan ZQ, Fuchs SY . Stability of homologue of Slimb F-box protein is regulated by availability of its substrate. J Biol Chem 2004; 279: 11074–11080. · DOI
  32. Wirbelauer C, Sutterluty H, Blondel M, Gstaiger M, Peter M, Reymond F et al. The F-box protein SKP2 is a ubiquitylation target of a CUL1-based core ubiquitin ligase complex: evidence for a role of CUL1 in the suppression of SKP2 expression in quiescent fibroblasts. EMBO J 2000; 19: 5362–5375. · DOI
  33. Wang W, Ungermannova D, Jin J, Harper JW, Liu X . Negative regulation of SCFSKP2 ubiquitin ligase by TGF-β signaling. Oncogene 2004; 23: 1064–1075. · DOI
  34. Listovsky T, Oren YS, Yudkovsky Y, Mahbubani HM, Weiss AM, Lebendiker M et al. Mammalian CDH1/FZR mediates its own degradation. EMBO J 2004; 23: 1619–1626. · DOI
  35. Pashkova N, Gakhar L, Winistorfer SC, Yu L, Ramaswamy S, Piper RC . WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol Cell 2010; 40: 433–443. · DOI
  36. Bennett EJ, Rush J, Gygi SP, Harper JW . Dynamics of Cullin-RING ubiquitin ligase network revealed by systemic quantitative proteomics. Cell 2010; 143: 951–965. · DOI
  37. Kamura T, Brower CS, Conaway RC, Conaway JW . A molecular basis for stabilization of the von Hippel-Lindau (VHL) tumor suppressor protein by components of the VHL ubiquitin ligase. J Biol Chem 2002; 277: 30388–30393. · DOI
  38. Zaaroor-Regev D, de Bie P, Scheffner M, Noy T, Shemer R, Heled M et al. Regulation of the polycomb protein RING1B by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome. Proc Natl Acad Sci USA 2010; 107: 6788–6793. · DOI
  39. Herman-Bachinsky Y, Ryoo HD, Ciechanover A, Gonen H . Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Cell Death Differ 2007; 14: 861–871. · DOI
  40. Silke J, Kratina T, Chu D, Ekert PG, Day CL, Pakusch M et al. Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance. Proc Natl Acad Sci USA 2005; 102: 16182–16187. · DOI
  41. Ditzel M, Wilson R, Tenev T, Zachariou A, Paul A, Deas E et al. Degradation of Diap1 by the N-end rule pathway is essential for regulating apoptosis. Nat Cell Biol 2003; 5: 467–473. · DOI
  42. Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM . The tumor autocrine motility factor receptor, GP78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 2001; 98: 14422–14427. · DOI
  43. Ballar P, Ors AU, Yang H, Fang S . Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases GP78 and HRD1. Int J Biochem Cell Biol 2010; 42: 167–173. · DOI
  44. Shmueli A, Tsai YC, Yang M, Braun MA, Weissman AM . Targeting of GP78 for ubiquitin-mediated proteasomal degradation by HRD1: cross-talk between E3s in the endoplasmic reticulum. Biochem Biophys Res Commun 2009; 390: 758–762. · DOI
  45. Courbard JR, Fiore F, Adelaide J, Borg JP, Birnbaum D, Ollendorff V . Interaction between two ubiquitin-protein isopeptide ligases of different classes, CBL-C and AIP4/ITCH. J Biol Chem 2002; 277: 45267–45275. · DOI
  46. Magnifico A, Ettenberg S, Yang C, Mariano J, Tiwari S, Fang S et al. WW domain HECT E3s target CBL RING finger E3s for proteasomal degradation. J Biol Chem 2003; 278: 43169–43177. · DOI
  47. Yang B, Gay DL, MacLeod MK, Cao X, Hala T, Sweezer EM et al. NEDD4 augments the adaptive immune response by promoting ubiquitin-mediated degradation of CBL-b in activated T cells. Nat Immunol 2008; 9: 1356–1363. · DOI
  48. Gruber T, Hermann-Kleiter N, Hinterleitner R, Fresser F, Schneider R, Gastl G et al. PKC-θ modulates the strength of T cell responses by targeting CBL-b for ubiquitination and degradation. Sci Signal 2009; 2: ra30. · DOI
  49. Bashir T, Dorrello NV, Amador V, Guardavaccaro D, Pagano M . Control of the SCF(SKP2-CKS1) ubiquitin ligase by the APC/C(CDH1) ubiquitin ligase. Nature 2004; 428: 190–193. · DOI
  50. Wei W, Ayad NG, Wan Y, Zhang GJ, Kirschner MW, Kaelin Jr WG . Degradation of the SCF component SKP2 in cell-cycle phase G1 by the anaphase-promoting complex. Nature 2004; 428: 194–198. · DOI
  51. Benmaamar R, Pagano M . Involvement of the SCF complex in the control of CDH1 degradation in S-phase. Cell Cycle 2005; 4: 1230–1232. · DOI
  52. Ayad NG, Rankin S, Murakami M, Jebanathirajah J, Gygi S, Kirschner MW . TOME-1, a trigger of mitotic entry, is degraded during G1 via the APC. Cell 2003; 113: 101–113. · DOI
  53. Nilsson J, Yekezare M, Minshull J, Pines J . The APC/C maintains the spindle assembly checkpoint by targeting Cdc20 for destruction. Nat Cell Biol 2008; 10: 1411–1420. · DOI
  54. Pfleger CM, Kirschner MW . The KEN box: an APC recognition signal distinct from the D box targeted by CDH1. Genes Dev 2000; 14: 655–665. · DOI
  55. Guardavaccaro D, Kudo Y, Boulaire J, Barchi M, Busino L, Donzelli M et al. Control of meiotic and mitotic progression by the F box protein β-TRCP1 in vivo. Dev Cell 2003; 4: 799–812. · DOI
  56. Margottin-Goguet F, Hsu JY, Loktev A, Hsieh HM, Reimann JD, Jackson PK . Prophase destruction of Emi1 by the SCF(β-TRCP/Slimb) ubiquitin ligase activates the anaphase promoting complex to allow progression beyond prometaphase. Dev Cell 2003; 4: 813–826. · DOI
  57. Wu-Baer F, Lagrazon K, Yuan W, Baer R . The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. J Biol Chem 2003; 278: 34743–34746. · DOI
  58. Mallery DL, Vandenberg CJ, Hiom K . Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J 2002; 21: 6755–6762. · DOI
  59. Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y et al. The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. J Biol Chem 2001; 276: 14537–14540. · DOI · Paper page
  60. Wang C, Deng L, Hong M, Akkaraju GR, Inoue J, Chen ZJ . TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 2001; 412: 346–351. · DOI · Paper page
  61. Baud V, Liu ZG, Bennett B, Suzuki N, Xia Y, Karin M . Signaling by proinflammatory cytokines: oligomerization of TRAF2 and TRAF6 is sufficient for JNK and IKK activation and target gene induction via an amino-terminal effector domain. Genes Dev 1999; 13: 1297–1308. · DOI
  62. Kanayama A, Seth RB, Sun L, Ea CK, Hong M, Shaito A et al. TAB2 and TAB3 activate the NF-κB pathway through binding to polyubiquitin chains. Mol Cell 2004; 15: 535–548. · DOI
  63. Sorrentino A, Thakur N, Grimsby S, Marcusson A, von Bulow V, Schuster N et al. The type I TGF-β receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat Cell Biol 2008; 10: 1199–1207. · DOI
  64. Fan Y, Yu Y, Shi Y, Sun W, Xie M, Ge N et al. Lysine 63-linked polyubiquitination of TAK1 at lysine 158 is required for tumor necrosis factor α- and interleukin-1β-induced IKK/NF-κB and JNK/AP-1 activation. J Biol Chem 2010; 285: 5347–5360. · DOI
  65. Xia ZP, Sun L, Chen X, Pineda G, Jiang X, Adhikari A et al. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature 2009; 461: 114–119. · DOI
  66. Lamothe B, Besse A, Campos AD, Webster WK, Wu H, Darnay BG . Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of IκB kinase activation. J Biol Chem 2007; 282: 4102–4112. · DOI
  67. Wu CJ, Conze DB, Li T, Srinivasula SM, Ashwell JD . Sensing of Lys 63-linked polyubiquitination by NEMO is a key event in NF-κB activation. Nat Cell Biol 2006; 8: 398–406. · DOI
  68. Woelk T, Oldrini B, Maspero E, Confalonieri S, Cavallaro E, Di Fiore PP et al. Molecular mechanisms of coupled monoubiquitination. Nat Cell Biol 2006; 8: 1246–1254. · DOI
  69. van Bergen En, Henegouwen PM . EPS15: a multifunctional adaptor protein regulating intracellular trafficking. Cell Commun Signal 2009; 7: 24. · DOI
  70. Daviet L, Colland F . Targeting ubiquitin specific proteases for drug discovery. Biochimie 2008; 90: 270–283. · DOI · Paper page
  71. de Bie P, Zaaroor-Regev D, Ciechanover A . Regulation of the polycomb protein RING1B ubiquitination by USP7. Biochem Biophys Res Commun 2010; 400: 389–395. · DOI
  72. Nathan JA, Sengupta S, Wood SA, Admon A, Markson G, Sanderson C et al. The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9X. Traffic 2008; 9: 1130–1145. · DOI · Paper page
  73. Maertens GN, El Messaoudi-Aubert S, Elderkin S, Hiom K, Peters G . Ubiquitin-specific proteases 7 and 11 modulate Polycomb regulation of the INK4a tumour suppressor. EMBO J 2010; 29: 2553–2565. · DOI
  74. Sun SC . CYLD: a tumor suppressor deubiquitinase regulating NF-κB activation and diverse biological processes. Cell Death Differ 2010; 17: 25–34. · DOI
  75. Boone DL, Turer EE, Lee EG, Ahmad RC, Wheeler MT, Tsui C et al. The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses. Nat Immunol 2004; 5: 1052–1060. · DOI
  76. Wertz IE, O’Rourke KM, Zhou H, Eby M, Aravind L, Seshagiri S et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling. Nature 2004; 430: 694–699. · DOI

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Metadata

Authors
de Bie, P., & Ciechanover, A.
Venue
Cell Death & Differentiation
Published
2011-03-04
Volume
18
Issue
9
Pages
1393-1402
ISSN
  • 1350-9047
  • 1476-5403
Cited by
296
References
4
Language
en

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