Ubiquitin becomes ubiquitous in cancer

References

• Ciechanover A, Elias S, Heller H, Ferber S, Hershko A. Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes. J Biol Chem 1980; 255:7525 - 7528
   PubMed Web of Science ®Google Scholar
• Ciechanover A, Heller H, Elias S, Haas AL, Hershko A. ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci USA 1980; 77:1365 - 1368
   PubMed Web of Science ®Google Scholar
• Nalepa G, Rolfe M, Harper JW. Drug discovery in the ubiquitin-proteasome system. Nat Rev Drug Discov 2006; 5:596 - 613
   PubMed Web of Science ®Google Scholar
• Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001; 70:503 - 533
   PubMed Web of Science ®Google Scholar
• Shi D, Pop MS, Kulikov R, Love IM, Kung AL, Grossman SR. CBP and p300 are cytoplasmic E4 polyubiquitin ligases for p53. Proc Natl Acad Sci USA 2009; 106:16275 - 16280
   PubMed Web of Science ®Google Scholar
• Hoppe T. Multiubiquitylation by E4 enzymes: ‘one size’ doesn't fit all. Trends Biochem Sci 2005; 30:183 - 187
   PubMed Web of Science ®Google Scholar
• Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 1999; 96:635 - 644
   PubMed Web of Science ®Google Scholar
• Hoege C, Pfander B, Moldovan GL, Pyrowolakis G, Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002; 419:135 - 141
   PubMed Web of Science ®Google Scholar
• Deng L, Wang C, Spencer E, Yang L, Braun A, You J, et al. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 2000; 103:351 - 361
   PubMed Web of Science ®Google Scholar
• Deshaies RJ, Joazeiro CA. RING domain E3 ubiquitin ligases. Annu Rev Biochem 2009; 78:399 - 434
   PubMed Web of Science ®Google Scholar
• Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, Seshagiri S, et al. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NFkappaB signalling. Nature 2004; 430:694 - 679
   PubMed Web of Science ®Google Scholar
• Reyes-Turcu FE, Ventii KH, Wilkinson KD. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 2009; 78:363 - 397
   PubMed Web of Science ®Google Scholar
• Futreal PA, Coin L, Marshall M, Down T, Hubbard T, Wooster R, et al. A census of human cancer genes. Nat Rev Cancer 2004; 4:177 - 183
   PubMed Web of Science ®Google Scholar
• Kruse JP, Gu W. Modes of p53 regulation. Cell 2009; 137:609 - 622
   PubMed Web of Science ®Google Scholar
• Scheffner M, Huibregtse JM, Vierstra RD, Howley PM. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 1993; 75:495 - 505
   PubMed Web of Science ®Google Scholar
• Scheffner M. Ubiquitin, E6-AP and their role in p53 inactivation. Pharmacol Ther 1998; 78:129 - 139
   PubMed Web of Science ®Google Scholar
• Giordano G, Azzoni C, D'Adda T, Rocco A, Gnetti L, Froio E, et al. Human papilloma virus (HPV) status, p16INK4a and p53 overexpression in epithelial malignant and borderline ovarian neoplasms. Pathol Res Pract 2008; 204:163 - 174
   PubMed Web of Science ®Google Scholar
• zur Hausen H. Papillomaviruses and cancer: from basic studies to clinical application. Nat Rev Cancer 2002; 2:342 - 350
   PubMed Web of Science ®Google Scholar
• Galani E, Christodoulou C. Human papilloma viruses and cancer in the post-vaccine era. Clin Microbiol Infect 2009; 15:977 - 981
   PubMed Web of Science ®Google Scholar
• de Rozieres S, Maya R, Oren M, Lozano G. The loss of mdm2 induces p53-mediated apoptosis. Oncogene 2000; 19:1691 - 1697
   PubMed Web of Science ®Google Scholar
• Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378:206 - 208
   PubMed Web of Science ®Google Scholar
• Momand J, Jung D, Wilczynski S, Niland J. The MDM2 gene amplification database. Nucleic Acids Res 1998; 26:3453 - 3459
   PubMed Web of Science ®Google Scholar
• Iwakuma T, Lozano G. MDM2, an introduction. Mol Cancer Res 2003; 1:993 - 1000
   PubMed Web of Science ®Google Scholar
• Quesnel B, Preudhomme C, Fournier J, Fenaux P, Peyrat JP. MDM2 gene amplification in human breast cancer. Eur J Cancer 1994; 30:982 - 984
   Web of Science ®Google Scholar
• Allende-Vega N, Saville MK. Targeting the ubiquitin-proteasome system to activate wild-type p53 for cancer therapy. Semin Cancer Biol 2010; 20:29 - 39
   PubMed Web of Science ®Google Scholar
• Cheok CF, Dey A, Lane DP. Cyclin-dependent kinase inhibitors sensitize tumor cells to nutlin-induced apoptosis: a potent drug combination. Mol Cancer Res 2007; 5:1133 - 1145
   PubMed Web of Science ®Google Scholar
• Tovar C, Rosinski J, Filipovic Z, Higgins B, Kolinsky K, Hilton H, et al. Small-molecule MDM2 antagonists reveal aberrant p53 signaling in cancer: implications for therapy. Proc Natl Acad Sci USA 2006; 103:1888 - 1893
   PubMed Web of Science ®Google Scholar
• Canner JA, Sobo M, Ball S, Hutzen B, DeAngelis S, Willis W, et al. MI-63: a novel small-molecule inhibitor targets MDM2 and induces apoptosis in embryonal and alveolar rhabdomyosarcoma cells with wild-type p53. Br J Cancer 2009; 101:774 - 781
   PubMed Web of Science ®Google Scholar
• Issaeva N, Bozko P, Enge M, Protopopova M, Verhoef LG, Masucci M, et al. Small molecule RITA binds to p53, blocks p53-HDM-2 interaction and activates p53 function in tumors. Nat Med 2004; 10:1321 - 1328
   PubMed Web of Science ®Google Scholar
• Li WD, Wang MJ, Ding F, Yin DL, Liu ZH. Cytotoxic effect of a non-peptidic small molecular inhibitor of the p53-HDM2 interaction on tumor cells. World J Gastroenterol 2005; 11:2927 - 2931
   PubMed Web of Science ®Google Scholar
• Chen D, Kon N, Li M, Zhang W, Qin J, Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005; 121:1071 - 1083
   PubMed Web of Science ®Google Scholar
• Chen D, Brooks CL, Gu W. ARF-BP1 as a potential therapeutic target. Br J Cancer 2006; 94:1555 - 1558
   PubMed Web of Science ®Google Scholar
• Dornan D, Bheddah S, Newton K, Ince W, Frantz GD, Dowd P, et al. COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas. Cancer Res 2004; 64:7226 - 7230
   PubMed Web of Science ®Google Scholar
• Leng RP, Lin Y, Ma W, Wu H, Lemmers B, Chung S, et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 2003; 112:779 - 791
   PubMed Web of Science ®Google Scholar
• Yamasaki S, Yagishita N, Sasaki T, Nakazawa M, Kato Y, Yamadera T, et al. Cytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase ‘Synoviolin’. EMBO J 2007; 26:113 - 122
   PubMed Web of Science ®Google Scholar
• Frescas D, Pagano M. Deregulated proteolysis by the F-box proteins SKP2 and beta-TrCP: tipping the scales of cancer. Nat Rev Cancer 2008; 8:438 - 449
   PubMed Web of Science ®Google Scholar
• Kipreos ET, Pagano M. The F-box protein family. Genome Biol 2000; 1:3002
   Google Scholar
• Cardozo T, Pagano M. The SCF ubiquitin ligase: insights into a molecular machine. Nat Rev Mol Cell Biol 2004; 5:739 - 751
   PubMed Web of Science ®Google Scholar
• Sutterluty H, Chatelain E, Marti A, Wirbelauer C, Senften M, Muller U, et al. p45SKP2 promotes p27Kip1 degradation and induces S phase in quiescent cells. Nat Cell Biol 1999; 1:207 - 214
   PubMed Web of Science ®Google Scholar
• Slingerland J, Pagano M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J Cell Physiol 2000; 183:10 - 17
   PubMed Web of Science ®Google Scholar
• Kiyokawa H, Kineman RD, Manova-Todorova KO, Soares VC, Hoffman ES, Ono M, et al. Enhanced growth of mice lacking the cyclin-dependent kinase inhibitor function of p27(Kip1). Cell 1996; 85:721 - 732
   PubMed Web of Science ®Google Scholar
• Nakayama K, Ishida N, Shirane M, Inomata A, Inoue T, Shishido N, et al. Mice lacking p27(Kip1) display increased body size, multiple organ hyperplasia, retinal dysplasia and pituitary tumors. Cell 1996; 85:707 - 720
   PubMed Web of Science ®Google Scholar
• Fero ML, Rivkin M, Tasch M, Porter P, Carow CE, Firpo E, et al. A syndrome of multiorgan hyperplasia with features of gigantism, tumorigenesis and female sterility in p27(Kip1)-deficient mice. Cell 1996; 85:733 - 744
   PubMed Web of Science ®Google Scholar
• Muraoka RS, Lenferink AE, Law B, Hamilton E, Brantley DM, Roebuck LR, et al. ErbB2/Neu-induced, cyclin D1-dependent transformation is accelerated in p27-haploinsufficient mammary epithelial cells but impaired in p27-null cells. Mol Cell Biol 2002; 22:2204 - 2219
   PubMed Web of Science ®Google Scholar
• Latres E, Chiarle R, Schulman BA, Pavletich NP, Pellicer A, Inghirami G, et al. Role of the F-box protein Skp2 in lymphomagenesis. Proc Natl Acad Sci USA 2001; 98:2515 - 2520
   PubMed Web of Science ®Google Scholar
• Shapira M, Ben-Izhak O, Linn S, Futerman B, Minkov I, Hershko DD. The prognostic impact of the ubiquitin ligase subunits Skp2 and Cks1 in colorectal carcinoma. Cancer 2005; 103:1336 - 1346
   PubMed Web of Science ®Google Scholar
• Traub F, Mengel M, Luck HJ, Kreipe HH, von Wasielewski R. Prognostic impact of Skp2 and p27 in human breast cancer. Breast Cancer Res Treat 2006; 99:185 - 191
   PubMed Web of Science ®Google Scholar
• Welcker M, Clurman BE. FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nat Rev Cancer 2008; 8:83 - 93
   PubMed Web of Science ®Google Scholar
• Yada M, Hatakeyama S, Kamura T, Nishiyama M, Tsunematsu R, Imaki H, et al. Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. EMBO J 2004; 23:2116 - 2125
   PubMed Web of Science ®Google Scholar
• Nateri AS, Riera-Sans L, Da Costa C, Behrens A. The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science 2004; 303:1374 - 1378
   PubMed Web of Science ®Google Scholar
• Oberg C, Li J, Pauley A, Wolf E, Gurney M, Lendahl U. The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. J Biol Chem 2001; 276:35847 - 35853
   PubMed Web of Science ®Google Scholar
• Mao JH, Kim IJ, Wu D, Climent J, Kang HC, DelRosario R, et al. FBXW7 targets mTOR for degradation and cooperates with PTEN in tumor suppression. Science 2008; 321:1499 - 1502
   PubMed Web of Science ®Google Scholar
• Koepp DM, Schaefer LK, Ye X, Keyomarsi K, Chu C, Harper JW, et al. Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 2001; 294:173 - 177
   PubMed Web of Science ®Google Scholar
• Mao JH, Perez-Losada J, Wu D, Delrosario R, Tsunematsu R, Nakayama KI, et al. Fbxw7/Cdc4 is a p53-dependent, haploinsufficient tumour suppressor gene. Nature 2004; 432:775 - 779
   PubMed Web of Science ®Google Scholar
• Lonser RR, Glenn GM, Walther M, Chew EY, Libutti SK, Linehan WM, et al. von Hippel-Lindau disease. Lancet 2003; 361:2059 - 2067
   PubMed Web of Science ®Google Scholar
• Latif F, Tory K, Gnarra J, Yao M, Duh FM, Orcutt ML, et al. Identification of the von Hippel-Lindau disease tumor suppressor gene. Science 1993; 260:1317 - 1320
   PubMed Web of Science ®Google Scholar
• Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, Cockman ME, et al. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 1999; 399:271 - 275
   PubMed Web of Science ®Google Scholar
• Hoeller D, Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 2009; 458:438 - 444
   PubMed Web of Science ®Google Scholar
• Kim WY, Kaelin WG. Role of VHL gene mutation in human cancer. J Clin Oncol 2004; 22:4991 - 5004
   PubMed Web of Science ®Google Scholar
• Semenza GL. HIF-1 and tumor progression: pathophysiology and therapeutics. Trends Mol Med 2002; 8:62 - 67
   PubMed Web of Science ®Google Scholar
• Ford D, Easton DF, Stratton M, Narod S, Goldgar D, Devilee P, et al. Genetic heterogeneity and penetrance analysis of the BRCA1 and BRCA2 genes in breast cancer families. The Breast Cancer Linkage Consortium. Am J Hum Genet 1998; 62:676 - 689
   PubMed Web of Science ®Google Scholar
• Scully R. Role of BRCA gene dysfunction in breast and ovarian cancer predisposition. Breast Cancer Res 2000; 2:324 - 330
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Ohta T, Fukuda M. Ubiquitin and breast cancer. Oncogene 2004; 23:2079 - 2088
   PubMed Web of Science ®Google Scholar
• Boulton SJ. BRCA1-mediated ubiquitylation. Cell Cycle 2006; 5:1481 - 1486
   PubMed Web of Science ®Google Scholar
• Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, et al. Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase. J Biol Chem 2004; 279:30919 - 30922
   PubMed Web of Science ®Google Scholar
• Starita LM, Horwitz AA, Keogh MC, Ishioka C, Parvin JD, Chiba N. BRCA1/BARD1 ubiquitinate phosphorylated RNA polymerase II. J Biol Chem 2005; 280:24498 - 24505
   PubMed Web of Science ®Google Scholar
• Yu X, Fu S, Lai M, Baer R, Chen J. BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP. Genes Dev 2006; 20:1721 - 1726
   PubMed Web of Science ®Google Scholar
• Chen C, Matesic LE. The Nedd4-like family of E3 ubiquitin ligases and cancer. Cancer Metastasis Rev 2007; 26:587 - 604
   PubMed Web of Science ®Google Scholar
• Wang X, Trotman LC, Koppie T, Alimonti A, Chen Z, Gao Z, et al. NEDD4-1 is a proto-oncogenic ubiquitin ligase for PTEN. Cell 2007; 128:129 - 139
   PubMed Web of Science ®Google Scholar
• Baker SJ. PTEN enters the nuclear age. Cell 2007; 128:25 - 28
   PubMed Web of Science ®Google Scholar
• Trotman LC, Wang X, Alimonti A, Chen Z, Teruya-Feldstein J, Yang H, et al. Ubiquitination regulates PTEN nuclear import and tumor suppression. Cell 2007; 128:141 - 156
   PubMed Web of Science ®Google Scholar
• Lian Z, Di Cristofano A. Class reunion: PTEN joins the nuclear crew. Oncogene 2005; 24:7394 - 7400
   PubMed Web of Science ®Google Scholar
• Fouladkou F, Landry T, Kawabe H, Neeb A, Lu C, Brose N, et al. The ubiquitin ligase Nedd4-1 is dispensable for the regulation of PTEN stability and localization. Proc Natl Acad Sci USA 2008; 105:8585 - 8590
   PubMed Web of Science ®Google Scholar
• Zhang Y, Chang C, Gehling DJ, Hemmati-Brivanlou A, Derynck R. Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase. Proc Natl Acad Sci USA 2001; 98:974 - 979
   PubMed Web of Science ®Google Scholar
• Kavsak P, Rasmussen RK, Causing CG, Bonni S, Zhu H, Thomsen GH, et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGFbeta receptor for degradation. Mol Cell 2000; 6:1365 - 1375
   PubMed Web of Science ®Google Scholar
• Lin X, Liang M, Feng XH. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling. J Biol Chem 2000; 275:36818 - 36822
   PubMed Web of Science ®Google Scholar
• Ikushima H, Miyazono K. TGFbeta signalling: a complex web in cancer progression. Nat Rev Cancer 2010; 10:415 - 424
   PubMed Web of Science ®Google Scholar
• Fukuchi M, Fukai Y, Masuda N, Miyazaki T, Nakajima M, Sohda M, et al. High-level expression of the Smad ubiquitin ligase Smurf2 correlates with poor prognosis in patients with esophageal squamous cell carcinoma. Cancer Res 2002; 62:7162 - 7165
   PubMed Web of Science ®Google Scholar
• Chen C, Sun X, Ran Q, Wilkinson KD, Murphy TJ, Simons JW, et al. Ubiquitin-proteasome degradation of KLF5 transcription factor in cancer and untransformed epithelial cells. Oncogene 2005; 24:3319 - 3327
   PubMed Web of Science ®Google Scholar
• Chen C, Zhou Z, Sheehan CE, Slodkowska E, Sheehan CB, Boguniewicz A, et al. Overexpression of WWP1 is associated with the estrogen receptor and insulin-like growth factor receptor 1 in breast carcinoma. Int J Cancer 2009; 124:2829 - 2836
   PubMed Web of Science ®Google Scholar
• Chen C, Sun X, Guo P, Dong XY, Sethi P, Cheng X, et al. Human Kruppel-like factor 5 is a target of the E3 ubiquitin ligase WWP1 for proteolysis in epithelial cells. J Biol Chem 2005; 280:41553 - 41561
   PubMed Web of Science ®Google Scholar
• Chen C, Bhalala HV, Vessella RL, Dong JT. KLF5 is frequently deleted and downregulated but rarely mutated in prostate cancer. Prostate 2003; 55:81 - 88
   PubMed Web of Science ®Google Scholar
• Chen C, Bhalala HV, Qiao H, Dong JT. A possible tumor suppressor role of the KLF5 transcription factor in human breast cancer. Oncogene 2002; 21:6567 - 6572
   PubMed Web of Science ®Google Scholar
• Laine A, Ronai Z. Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1. Oncogene 2007; 26:1477 - 1483
   PubMed Web of Science ®Google Scholar
• Holowaty MN, Zeghouf M, Wu H, Tellam J, Athanasopoulos V, Greenblatt J, et al. Protein profiling with Epstein-Barr nuclear antigen-1 reveals an interaction with the herpesvirus-associated ubiquitin-specific protease HAUSP/USP7. J Biol Chem 2003; 278:29987 - 29994
   PubMed Web of Science ®Google Scholar
• Meredith M, Orr A, Everett R. Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135 kDa cellular protein. Virology 1994; 200:457 - 469
   PubMed Web of Science ®Google Scholar
• Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J, et al. Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 2002; 416:648 - 653
   PubMed Web of Science ®Google Scholar
• Li M, Brooks CL, Kon N, Gu W. A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 2004; 13:879 - 886
   PubMed Web of Science ®Google Scholar
• Cummins JM, Rago C, Kohli M, Kinzler KW, Lengauer C, Vogelstein B. Tumour suppression: disruption of HAUSP gene stabilizes p53. Nature 2004; 428:486
   PubMed Web of Science ®Google Scholar
• Meulmeester E, Maurice MM, Boutell C, Teunisse AF, Ovaa H, Abraham TE, Dirks RW, Jochemensen AG. Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2. Mol Cell 2005; 18:565 - 576
   PubMed Web of Science ®Google Scholar
• van der Horst A, de Vries-Smits AM, Brenkman AB, van Triest MH, van den Broek N, Colland F, et al. FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP. Nat Cell Biol 2006; 8:1064 - 1073
   PubMed Web of Science ®Google Scholar
• Song MS, Salmena L, Carracedo A, Egia A, Lo-Coco F, Teruya-Feldstein J, et al. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature 2008; 455:813 - 817
   PubMed Web of Science ®Google Scholar
• Colland F. Ubiquitin and cancer: from molecular targets and mechanisms to the clinic—AACR Special Conference. IDrugs 2006; 9:179 - 181
   PubMed Web of Science ®Google Scholar
• Colland F, Formstecher E, Jacq X, Reverdy C, Planquette C, Conrath S, et al. Small-molecule inhibitor of USP7/HAUSP ubiquitin protease stabilizes and activates p53 in cells. Mol Cancer Ther 2009; 8:2286 - 2295
   PubMed Web of Science ®Google Scholar
• Gousseva N, Baker RT. Gene structure, alternate splicing, tissue distribution, cellular localization and developmental expression pattern of mouse deubiquitinating enzyme isoforms Usp2-45 and Usp2-69. Gene Expr 2003; 11:163 - 179
   PubMed Web of Science ®Google Scholar
• Graner E, Tang D, Rossi S, Baron A, Migita T, Weinstein LJ, et al. The isopeptidase USP2a regulates the stability of fatty acid synthase in prostate cancer.. Cancer Cell 2004; 5:253 - 261
   PubMed Web of Science ®Google Scholar
• Oishi K, Miyazaki K, Kadota K, Kikuno R, Nagase T, Atsumi G, et al. Genome-wide expression analysis of mouse liver reveals CLOCK-regulated circadian output genes. J Biol Chem 2003; 278:41519 - 41527
   PubMed Web of Science ®Google Scholar
• Stevenson LF, Sparks A, Allende-Vega N, Xirodimas DP, Lane DP, Saville MK. The deubiquitinating enzyme USP2a regulates the p53 pathway by targeting Mdm2. EMBO J 2007; 26:976 - 986
   PubMed Web of Science ®Google Scholar
• Allende-Vega N, Sparks A, Lane DP, Saville MK. MdmX is a substrate for the deubiquitinating enzyme USP2a. Oncogene 2010; 29:432 - 441
   PubMed Web of Science ®Google Scholar
• Priolo C, Tang D, Brahamandan M, Benassi B, Sicinska E, Ogino S, et al. The isopeptidase USP2a protects human prostate cancer from apoptosis. Cancer Res 2006; 66:8625 - 8632
   PubMed Web of Science ®Google Scholar
• Albihn A, Johnsen JI, Henriksson MA. MYC in oncogenesis and as a target for cancer therapies. Adv Cancer Res 2010; 107:163 - 224
   PubMed Web of Science ®Google Scholar
• Amati B, Sanchez-Arevalo Lobo VJ. MYC degradation: deubiquitinating enzymes enter the dance. Nat Cell Biol 2007; 9:729 - 731
   PubMed Web of Science ®Google Scholar
• Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, et al. The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc Natl Acad Sci USA 2004; 101:9085 - 9090
   PubMed Web of Science ®Google Scholar
• Popov N, Wanzel M, Madiredjo M, Zhang D, Beijersbergen R, Bernards R, et al. The ubiquitin-specific protease USP28 is required for MYC stability. Nat Cell Biol 2007; 9:765 - 774
   PubMed Web of Science ®Google Scholar
• Zhang D, Zaugg K, Mak TW, Elledge SJ. A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response. Cell 2006; 126:529 - 542
   PubMed Web of Science ®Google Scholar
• Bignell GR, Warren W, Seal S, Takahashi M, Rapley E, Barfoot R, et al. Identification of the familial cylindromatosis tumour-suppressor gene. Nat Genet 2000; 25:160 - 165
   PubMed Web of Science ®Google Scholar
• Yoshida H, Jono H, Kai H, Li JD. The tumor suppressor cylindromatosis (CYLD) acts as a negative regulator for toll-like receptor 2 signaling via negative crosstalk with TRAF6 AND TRAF7. J Biol Chem 2005; 280:41111 - 41121
   PubMed Web of Science ®Google Scholar
• Jono H, Lim JH, Chen LF, Xu H, Trompouki E, Pan ZK, et al. NFkappaB is essential for induction of CYLD, the negative regulator of NFkappaB: evidence for a novel inducible autoregulatory feedback pathway. J Biol Chem 2004; 279:36171 - 36174
   PubMed Web of Science ®Google Scholar
• Komander D, Lord CJ, Scheel H, Swift S, Hofmann K, Ashworth A, et al. The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module. Mol Cell 2008; 29:451 - 464
   PubMed Web of Science ®Google Scholar
• Brummelkamp TR, Nijman SM, Dirac AM, Bernards R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NFkappaB. Nature 2003; 424:797 - 801
   PubMed Web of Science ®Google Scholar
• Kovalenko A, Chable-Bessia C, Cantarella G, Israel A, Wallach D, Courtois G. The tumour suppressor CYLD negatively regulates NFkappaB signalling by deubiquitination. Nature 2003; 424:801 - 815
   PubMed Web of Science ®Google Scholar
• Reiley WW, Jin W, Lee AJ, Wright A, Wu X, Tewalt EF, et al. Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses. J Exp Med 2007; 204:1475 - 1485
   PubMed Web of Science ®Google Scholar
• Massoumi R, Chmielarska K, Hennecke K, Pfeifer A, Fassler R. Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NFkappaB signaling. Cell 2006; 125:665 - 677
   PubMed Web of Science ®Google Scholar
• Sun SC. CYLD: a tumor suppressor deubiquitinase regulating NFkappaB activation and diverse biological processes. Cell Death Differ 2010; 17:25 - 34
   PubMed Web of Science ®Google Scholar
• Sacco JJ, Coulson JM, Clague MJ, Urbe S. Emerging roles of deubiquitinases in cancer-associated pathways. IUBMB Life 2010; 62:140 - 157
   PubMed Web of Science ®Google Scholar
• Hitotsumatsu O, Ahmad RC, Tavares R, Wang M, Philpott D, Turer EE, et al. The ubiquitin-editing enzyme A20 restricts nucleotide-binding oligomerization domain containing 2-triggered signals. Immunity 2008; 28:381 - 390
   PubMed Web of Science ®Google Scholar
• Turer EE, Tavares RM, Mortier E, Hitotsumatsu O, Advincula R, Lee B, et al. Homeostatic MyD88-dependent signals cause lethal inflamMation in the absence of A20. J Exp Med 2008; 205:451 - 464
   PubMed Web of Science ®Google Scholar
• Duwel M, Welteke V, Oeckinghaus A, Baens M, Kloo B, Ferch U, et al. A20 negatively regulates T cell receptor signaling to NFkappaB by cleaving Malt1 ubiquitin chains. J Immunol 2009; 182:7718 - 7728
   PubMed Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Mauro C, Pacifico F, Lavorgna A, Mellone S, Iannetti A, Acquaviva R, et al. ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NFkappaB. J Biol Chem 2006; 281:18482 - 18488
   PubMed Web of Science ®Google Scholar
• Lee EG, Boone DL, Chai S, Libby SL, Chien M, Lodolce JP, et al. Failure to regulate TNF-induced NFkappaB and cell death responses in A20-deficient mice. Science 2000; 289:2350 - 2354
   PubMed Web of Science ®Google Scholar
• Song HY, Rothe M, Goeddel DV. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NFkappaB activation. Proc Natl Acad Sci USA 1996; 93:6721 - 6725
   PubMed Web of Science ®Google Scholar
• Li L, Soetandyo N, Wang Q, Ye Y. The zinc finger protein A20 targets TRAF2 to the lysosomes for degradation. Biochim Biophys Acta 2009; 1793:346 - 353
   PubMed Web of Science ®Google Scholar
• Schmitz R, Hansmann ML, Bohle V, Martin-Subero JI, Hartmann S, Mechtersheimer G, et al. TNFAIP3 (A20) is a tumor suppressor gene in Hodgkin lymphoma and primary mediastinal B cell lymphoma. J Exp Med 2009; 206:981 - 989
   PubMed Web of Science ®Google Scholar
• Hymowitz SG, Wertz IE. A20: from ubiquitin editing to tumour suppression. Nat Rev Cancer 2010; 10:332 - 341
   PubMed Web of Science ®Google Scholar
• Huang Y, Baker RT, Fischer-Vize JA. Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science 1995; 270:1828 - 1831
   PubMed Web of Science ®Google Scholar
• Murray RZ, Jolly LA, Wood SA. The FAM deubiquitylating enzyme localizes to multiple points of protein trafficking in epithelia, where it associates with E-cadherin and beta-catenin. Mol Biol Cell 2004; 15:1591 - 1599
   PubMed Web of Science ®Google Scholar
• Dupont S, Mamidi A, Cordenonsi M, Montagner M, Zacchigna L, Adorno M, et al. FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination. Cell 2009; 136:123 - 135
   PubMed Web of Science ®Google Scholar
• Schwickart M, Huang X, Lill JR, Liu J, Ferrando R, French DM, et al. Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival. Nature 2010; 463:103 - 107
   PubMed Web of Science ®Google Scholar
• Mishra A, Godavarthi SK, Jana NR. UBE3A/E6-AP regulates cell proliferation by promoting proteasomal degradation of p27. Neurobiol Dis 2009; 36:26 - 34
   PubMed Web of Science ®Google Scholar
• Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387:296 - 299
   PubMed Web of Science ®Google Scholar
• Schlott T, Reimer S, Jahns A, Ohlenbusch A, Ruschenburg I, Nagel H, et al. Point mutations and nucleotide insertions in the MDM2 zinc finger structure of human tumours. J Pathol 1997; 182:54 - 61
   PubMed Web of Science ®Google Scholar
• Hershko DD. Oncogenic properties and prognostic implications of the ubiquitin ligase Skp2 in cancer. Cancer 2008; 112:1415 - 1424
   PubMed Web of Science ®Google Scholar
• Akhoondi S, Sun D, von der Lehr N, Apostolidou S, Klotz K, Maljukova A, et al. FBXW7/hCDC4 is a general tumor suppressor in human cancer. Cancer Res 2007; 67:9006 - 9012
   PubMed Web of Science ®Google Scholar
• Hogervorst FB, Nederlof PM, Gille JJ, McElgunn CJ, Grippeling M, Pruntel R, et al. Large genomic deletions and duplications in the BRCA1 gene identified by a novel quantitative method. Cancer Res 2003; 63:1449 - 1453
   PubMed Web of Science ®Google Scholar
• Esteller M, Silva JM, Dominguez G, Bonilla F, Matias-Guiu X, Lerma E, et al. Promoter hypermethylation and BRCA1 inactivation in sporadic breast and ovarian tumors. J Natl Cancer Inst 2000; 92:564 - 569
   PubMed Web of Science ®Google Scholar
• Strack B, Calistri A, Accola MA, Palu G, Gottlinger HG. A role for ubiquitin ligase recruitment in retrovirus release. Proc Natl Acad Sci USA 2000; 97:13063 - 13068
   PubMed Web of Science ®Google Scholar
• Kim SS, Yoo NJ, Jeong EG, Kim MS, Lee SH. Expression of NEDD4-1, a PTEN regulator, in gastric and colorectal carcinomas. APMIS 2008; 116:779 - 784
   PubMed Web of Science ®Google Scholar
• Chen C, Zhou Z, Guo P, Dong JT. Proteasomal degradation of the KLF5 transcription factor through a ubiquitin-independent pathway. FEBS Lett 2007; 581:1124 - 1130
   PubMed Web of Science ®Google Scholar
• Li Y, Zhou Z, Chen C. WW domain-containing E3 ubiquitin protein ligase 1 targets p63 transcription factor for ubiquitin-mediated proteasomal degradation and regulates apoptosis. Cell Death Differ 2008; 15:1941 - 1951
   PubMed Web of Science ®Google Scholar
• Li Y, Zhou Z, Alimandi M, Chen C. WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer. Oncogene 2009; 28:2948 - 2958
   PubMed Web of Science ®Google Scholar
• Chen C, Sun X, Guo P, Dong XY, Sethi P, Zhou W, et al. Ubiquitin E3 ligase WWP1 as an oncogenic factor in human prostate cancer. Oncogene 2007; 26:2386 - 2394
   PubMed Web of Science ®Google Scholar
• Chen C, Zhou Z, Ross JS, Zhou W, Dong JT. The amplified WWP1 gene is a potential molecular target in breast cancer. Int J Cancer 2007; 121:80 - 87
   PubMed Web of Science ®Google Scholar
• Becker K, Marchenko ND, Palacios G, Moll UM. A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model. Cell Cycle 2008; 7:1205 - 1213
   PubMed Web of Science ®Google Scholar
• Masuya D, Huang C, Liu D, Nakashima T, Yokomise H, Ueno M, et al. The HAUSP gene plays an important role in non-small cell lung carcinogenesis through p53-dependent pathways. J Pathol 2006; 208:724 - 732
   PubMed Web of Science ®Google Scholar
• Novak U, Rinaldi A, Kwee I, Nandula SV, Rancoita PM, Compagno M, et al. The NF-{kappa}B negative regulator TNFAIP3 (A20) is inactivated by somatic mutations and genomic deletions in marginal zone lymphomas. Blood 2009; 113:4918 - 4921
   PubMed Web of Science ®Google Scholar
• Chanudet E, Huang Y, Ichimura K, Dong G, Hamoudi RA, Radford J, et al. A20 is targeted by promoter methylation, deletion and inactivating mutation in MALT lymphoma. Leukemia 2010; 24:483 - 487
   PubMed Web of Science ®Google Scholar
• Chanudet E, Ye H, Ferry J, Bacon CM, Adam P, Muller-Hermelink HK, et al. A20 deletion is associated with copy number gain at the TNFA/B/C locus and occurs preferentially in translocation-negative MALT lymphoma of the ocular adnexa and salivary glands. J Pathol 2009; 217:420 - 430
   PubMed Web of Science ®Google Scholar
• Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, et al. Overexpression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics. Breast Cancer Res Treat 2007; 104:21 - 30
   PubMed Web of Science ®Google Scholar