Artemis interacts with the Cul4A-DDB1^DDB2 ubiquitin E3 ligase and regulates degradation of the CDK inhibitor p27

References

• Bonatto D, Revers LF, Brendel M, Henriques JA. The eukaryotic Pso2/Snm1/Artemis proteins and their function as genomic and cellular caretakers. Braz J Med Biol Res 2005; 38:321 - 334; PMID: 15761611; http://dx.doi.org/10.1590/S0100-879X2005000300002
   PubMed Web of Science ®Google Scholar
• Cattell E, Sengerova B, McHugh PJ. The SNM1/Pso2 family of ICL repair nucleases: From yeast to man. Environ Mol Mutagen 2010; 51:635 - 645; PMID: 20175117
   PubMed Web of Science ®Google Scholar
• Dominski Z. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol 2007; 42:67 - 93; PMID: 17453916; http://dx.doi.org/10.1080/10409230701279118
   PubMed Web of Science ®Google Scholar
• Yu Y, Mahaney BL, Yano K, Ye R, Fang S, Douglas P, et al. DNA-PK and ATM phosphorylation sites in XLF/Cernunnos are not required for repair of DNA double strand breaks. DNA Repair (Amst) 2008; 7:1680 - 1692; PMID: 18644470; http://dx.doi.org/10.1016/j.dnarep.2008.06.015
   PubMed Web of Science ®Google Scholar
• Yan Y, Akhter S, Zhang X, Legerski R. The multifunctional SNM1 gene family: not just nucleases. Future Oncol 2010; 6:1015 - 1029; PMID: 20528238; http://dx.doi.org/10.2217/fon.10.47
   PubMed Web of Science ®Google Scholar
• Callebaut I, Moshous D, Mornon JP, de Villartay JP. Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family. Nucleic Acids Res 2002; 30:3592 - 3601; PMID: 12177301; http://dx.doi.org/10.1093/nar/gkf470
   PubMed Web of Science ®Google Scholar
• Moshous D, Callebaut I, de Chasseval R, Corneo B, Cavazzana-Calvo M, Le Deist F, et al. Artemis, a novel DNA double-strand break repair/V(D)J recombination protein, is mutated in human severe combined immune deficiency. Cell 2001; 105:177 - 186; PMID: 11336668; http://dx.doi.org/10.1016/S0092-8674(01)00309-9
   PubMed Web of Science ®Google Scholar
• Akhter S, Lam YC, Chang S, Legerski RJ. The telomeric protein SNM1B/Apollo is required for normal cell proliferation and embryonic development. Aging Cell 2010; 9:1047 - 1056; PMID: 20854421; http://dx.doi.org/10.1111/j.1474-9726.2010.00631.x
   PubMed Web of Science ®Google Scholar
• Lam YC, Akhter S, Gu P, Ye J, Poulet A, Giraud-Panis MJ, et al. SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated repair. EMBO J 2010; 29:2230 - 2241; PMID: 20551906; http://dx.doi.org/10.1038/emboj.2010.58
   PubMed Web of Science ®Google Scholar
• Riballo E, Kuhne M, Rief N, Doherty A, Smith GC, Recio MJ, et al. A pathway of double-strand break rejoining dependent upon ATM, Artemis and proteins locating to gamma-H2AX foci. Mol Cell 2004; 16:715 - 724; PMID: 15574327; http://dx.doi.org/10.1016/j.molcel.2004.10.029
   PubMed Web of Science ®Google Scholar
• Wakasugi M, Kawashima A, Morioka H, Linn S, Sancar A, Mori T, et al. DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair. J Biol Chem 2002; 277:1637 - 1640; PMID: 11705987; http://dx.doi.org/10.1074/jbc.C100610200
   PubMed Web of Science ®Google Scholar
• Cavazzana-Calvo M, Le Deist F, De Saint Basile G, Papadopoulo D, De Villartay JP, Fischer A. Increased radiosensitivity of granulocyte macrophage colony-forming units and skin fibroblasts in human autosomal recessive severe combined immunodeficiency. J Clin Invest 1993; 91:1214 - 1218; PMID: 8450050; http://dx.doi.org/10.1172/JCI116282
   PubMed Web of Science ®Google Scholar
• Moshous D, Li L, Chasseval R, Philippe N, Jabado N, Cowan MJ, et al. A new gene involved in DNA double-strand break repair and V(D)J recombination is located on human chromosome 10p. Hum Mol Genet 2000; 9:583 - 588; PMID: 10699181; http://dx.doi.org/10.1093/hmg/9.4.583
   PubMed Web of Science ®Google Scholar
• Akhter S, Richie CT, Deng JM, Brey E, Zhang X, Patrick C Jr, et al. Deficiency in SNM1 abolishes an early mitotic checkpoint induced by spindle stress. Mol Cell Biol 2004; 24:10448 - 10455; PMID: 15542852; http://dx.doi.org/10.1128/MCB.24.23.10448-55.2004
   PubMed Web of Science ®Google Scholar
• Liu L, Akhter S, Bae JB, Mukhopadhyay SS, Richie CT, Liu X, et al. SNM1B/Apollo interacts with astrin and is required for the prophase cell cycle checkpoint. Cell Cycle 2009; 8:628 - 638; PMID: 19197158; http://dx.doi.org/10.4161/cc.8.4.7791
   PubMed Web of Science ®Google Scholar
• Geng L, Zhang X, Zheng S, Legerski RJ. Artemis links ATM to G2/M checkpoint recovery via regulation of Cdk1-cyclin B. Mol Cell Biol 2007; 27:2625 - 2635; PMID: 17242184; http://dx.doi.org/10.1128/MCB.02072-06
   PubMed Web of Science ®Google Scholar
• Wang H, Zhang X, Geng L, Teng L, Legerski RJ. Artemis regulates cell cycle recovery from the S phase checkpoint by promoting degradation of cyclin E. J Biol Chem 2009; 284:18236 - 18243; PMID: 19423708; http://dx.doi.org/10.1074/jbc.M109.002584
   PubMed Web of Science ®Google Scholar
• Zhang X, Succi J, Feng Z, Prithivirajsingh S, Story MD, Legerski RJ. Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response. Mol Cell Biol 2004; 24:9207 - 9220; PMID: 15456891; http://dx.doi.org/10.1128/MCB.24.20.9207-20.2004
   PubMed Web of Science ®Google Scholar
• Zhang X, Zhu Y, Geng L, Wang H, Legerski RJ. Artemis is a negative regulator of p53 in response to oxidative stress. Oncogene 2009; 28:2196 - 2204; PMID: 19398950; http://dx.doi.org/10.1038/onc.2009.100
   PubMed Web of Science ®Google Scholar
• Borriello A, Cucciolla V, Oliva A, Zappia V, Della Ragione F. p27Kip1 metabolism: a fascinating labyrinth. Cell Cycle 2007; 6:1053 - 1061; PMID: 17426451; http://dx.doi.org/10.4161/cc.6.9.4142
   PubMed Web of Science ®Google Scholar
• Cánepa ET, Scassa ME, Ceruti JM, Marazita MC, Carcagno AL, Sirkin PF, et al. INK4 proteins, a family of mammalian CDK inhibitors with novel biological functions. IUBMB Life 2007; 59:419 - 426; PMID: 17654117; http://dx.doi.org/10.1080/15216540701488358
   PubMed Web of Science ®Google Scholar
• Alkarain A, Jordan R, Slingerland J. p27 deregulation in breast cancer: prognostic significance and implications for therapy. J Mammary Gland Biol Neoplasia 2004; 9:67 - 80; PMID: 15082919; http://dx.doi.org/10.1023/B:JOMG.0000023589.00994.5e
   PubMed Web of Science ®Google Scholar
• Alkarain A, Slingerland J. Deregulation of p27 by oncogenic signaling and its prognostic significance in breast cancer. Breast Cancer Res 2004; 6:13 - 21; PMID: 14680481; http://dx.doi.org/10.1186/bcr722
   PubMed Web of Science ®Google Scholar
• Lee J, Kim SS. The function of p27KIP1 during tumor development. Exp Mol Med 2009; 41:765 - 771; PMID: 19887899; http://dx.doi.org/10.3858/emm.2009.41.11.102
   PubMed Web of Science ®Google Scholar
• Guan X, Wang Y, Xie R, Chen L, Bai J, Lu J, et al. p27 as a prognostic factor in breast cancer: a systematic review and meta-analysis. J Cell Mol Med 2010; 14:944 - 953; PMID: 19298520; http://dx.doi.org/10.1111/j.1582-4934.2009.00730.x
   PubMed Web of Science ®Google Scholar
• Belletti B, Nicoloso MS, Schiappacassi M, Chimienti E, Berton S, Lovat F, et al. p27(kip1) functional regulation in human cancer: a potential target for therapeutic designs. Curr Med Chem 2005; 12:1589 - 1605; PMID: 16022660; http://dx.doi.org/10.2174/0929867054367149
   PubMed Web of Science ®Google Scholar
• Carrano AC, Eytan E, Hershko A, Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999; 1:193 - 199; PMID: 10559916; http://dx.doi.org/10.1038/12013
   PubMed Web of Science ®Google Scholar
• Sutterlüty 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; PMID: 10559918; http://dx.doi.org/10.1038/12027
   PubMed Web of Science ®Google Scholar
• Tsvetkov LM, Yeh KH, Lee SJ, Sun H, Zhang H. p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr Biol 1999; 9:661 - 664; PMID: 10375532; http://dx.doi.org/10.1016/S0960-9822(99)80290-5
   PubMed Web of Science ®Google Scholar
• Kamura T, Hara T, Matsumoto M, Ishida N, Okumura F, Hatakeyama S, et al. Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nat Cell Biol 2004; 6:1229 - 1235; PMID: 15531880; http://dx.doi.org/10.1038/ncb1194
   PubMed Web of Science ®Google Scholar
• Bondar T, Kalinina A, Khair L, Kopanja D, Nag A, Bagchi S, et al. Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome. Mol Cell Biol 2006; 26:2531 - 2539; PMID: 16537899; http://dx.doi.org/10.1128/MCB.26.7.2531-9.2006
   PubMed Web of Science ®Google Scholar
• Li B, Jia N, Kapur R, Chun KT. Cul4A targets p27 for degradation and regulates proliferation, cell cycle exit and differentiation during erythropoiesis. Blood 2006; 107:4291 - 4299; PMID: 16467204; http://dx.doi.org/10.1182/blood-2005-08-3349
   PubMed Web of Science ®Google Scholar
• Higa LA, Yang X, Zheng J, Banks D, Wu M, Ghosh P, et al. Involvement of CUL4 ubiquitin E3 ligases in regulating CDK inhibitors Dacapo/p27Kip1 and cyclin E degradation. Cell Cycle 2006; 5:71 - 77; PMID: 16322693; http://dx.doi.org/10.4161/cc.5.1.2266
   PubMed Web of Science ®Google Scholar
• Groisman R, Polanowska J, Kuraoka I, Sawada J, Saijo M, Drapkin R, et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 2003; 113:357 - 367; PMID: 12732143; http://dx.doi.org/10.1016/S0092-8674(03)00316-7
   PubMed Web of Science ®Google Scholar
• McCall CM, Hu J, Xiong Y. Recruiting substrates to cullin 4-dependent ubiquitin ligases by DDB1. Cell Cycle 2005; 4:27 - 29; PMID: 15655366; http://dx.doi.org/10.4161/cc.4.1.1396
   PubMed Web of Science ®Google Scholar
• O'Connell BC, Harper JW. Ubiquitin proteasome system (UPS): what can chromatin do for you?. Curr Opin Cell Biol 2007; 19:206 - 214; PMID: 17314036; http://dx.doi.org/10.1016/j.ceb.2007.02.014
   PubMed Web of Science ®Google Scholar
• Jin J, Arias EE, Chen J, Harper JW, Walter JC. A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1. Mol Cell 2006; 23:709 - 721; PMID: 16949367; http://dx.doi.org/10.1016/j.molcel.2006.08.010
   PubMed Web of Science ®Google Scholar
• Lee J, Zhou P. DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase. Mol Cell 2007; 26:775 - 780; PMID: 17588513; http://dx.doi.org/10.1016/j.molcel.2007.06.001
   PubMed Web of Science ®Google Scholar
• Chu G, Chang E. Xeroderma pigmentosum group E cells lack a nuclear factor that binds to damaged DNA. Science 1988; 242:564 - 567; PMID: 3175673; http://dx.doi.org/10.1126/science.3175673
   PubMed Web of Science ®Google Scholar
• Hwang BJ, Chu G. Purification and characterization of a human protein that binds to damaged DNA. Biochemistry 1993; 32:1657 - 1666; PMID: 8431446; http://dx.doi.org/10.1021/bi00057a033
   PubMed Web of Science ®Google Scholar
• Hwang BJ, Ford JM, Hanawalt PC, Chu G. Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair. Proc Natl Acad Sci USA 1999; 96:424 - 428; PMID: 9892649; http://dx.doi.org/10.1073/pnas.96.2.424
   PubMed Web of Science ®Google Scholar
• Wang H, Zhai L, Xu J, Joo HY, Jackson S, Erdjument-Bromage H, et al. Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage. Mol Cell 2006; 22:383 - 394; PMID: 16678110; http://dx.doi.org/10.1016/j.molcel.2006.03.035
   PubMed Web of Science ®Google Scholar
• Sugasawa K, Okuda Y, Saijo M, Nishi R, Matsuda N, Chu G, et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 2005; 121:387 - 400; PMID: 15882621; http://dx.doi.org/10.1016/j.cell.2005.02.035
   PubMed Web of Science ®Google Scholar
• Nag A, Bondar T, Shiv S, Raychaudhuri P. The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells. Mol Cell Biol 2001; 21:6738 - 6747; PMID: 11564859; http://dx.doi.org/10.1128/MCB.21.20.6738-47.2001
   PubMed Web of Science ®Google Scholar
• Chandramohan V, Mineva ND, Burke B, Jeay S, Wu M, Shen J, et al. c-Myc represses FOXO3a-mediated transcription of the gene encoding the p27(Kip1) cyclin dependent kinase inhibitor. J Cell Biochem 2008; 104:2091 - 2106; PMID: 18393360; http://dx.doi.org/10.1002/jcb.21765
   PubMed Web of Science ®Google Scholar
• Chassot AA, Turchi L, Virolle T, Fitsialos G, Batoz M, Deckert M, et al. Id3 is a novel regulator of p27kip1 mRNA in early G1 phase and is required for cell cycle progression. Oncogene 2007; 26:5772 - 5783; PMID: 17404577; http://dx.doi.org/10.1038/sj.onc.1210386
   PubMed Web of Science ®Google Scholar
• Wang C, Hou X, Mohapatra S, Ma Y, Cress WD, Pledger WJ, et al. Activation of p27Kip1 Expression by E2F1. A negative feedback mechanism. J Biol Chem 2005; 280:12339 - 12343; PMID: 15713665; http://dx.doi.org/10.1074/jbc.C400536200
   PubMed Web of Science ®Google Scholar
• Wei D, Kanai M, Jia Z, Le X, Xie K. Kruppel-like factor 4 induces p27Kip1 expression in and suppresses the growth and metastasis of human pancreatic cancer cells. Cancer Res 2008; 68:4631 - 4639; PMID: 18559508; http://dx.doi.org/10.1158/0008-5472.CAN-07-5953
   PubMed Web of Science ®Google Scholar
• Sheaff RJ, Groudine M, Gordon M, Roberts JM, Clurman BE. Cyclin E-CDK2 is a regulator of p27Kip1. Genes Dev 1997; 11:1464 - 1478; PMID: 9192873; http://dx.doi.org/10.1101/gad.11.11.1464
   PubMed Web of Science ®Google Scholar
• Montagnoli A, Fiore F, Eytan E, Carrano AC, Draetta GF, Hershko A, et al. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev 1999; 13:1181 - 1189; PMID: 10323868; http://dx.doi.org/10.1101/gad.13.9.1181
   PubMed Web of Science ®Google Scholar
• Liang J, Zubovitz J, Petrocelli T, Kotchetkov R, Connor MK, Han K, et al. PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest. Nat Med 2002; 8:1153 - 1160; PMID: 12244302; http://dx.doi.org/10.1038/nm761
   PubMed Web of Science ®Google Scholar
• Jackson S, Xiong Y. CRL4s: the CUL4-RING E3 ubiquitin ligases. Trends Biochem Sci 2009; 34:562 - 570; PMID: 19818632; http://dx.doi.org/10.1016/j.tibs.2009.07.002
   PubMed Web of Science ®Google Scholar
• Hu J, McCall CM, Ohta T, Xiong Y. Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage. Nat Cell Biol 2004; 6:1003 - 1009; PMID: 15448697; http://dx.doi.org/10.1038/ncb1172
   PubMed Web of Science ®Google Scholar
• Coats S, Flanagan WM, Nourse J, Roberts JM. Requirement of p27Kip1 for restriction point control of the fibroblast cell cycle. Science 1996; 272:877 - 880; PMID: 8629023; http://dx.doi.org/10.1126/science.272.5263.877
   PubMed Web of Science ®Google Scholar
• Bodnar AG, Ouellette M, Frolkis M, Holt SE, Chiu CP, Morin GB, et al. Extension of life-span by introduction of telomerase into normal human cells. Science 1998; 279:349 - 352; PMID: 9454332; http://dx.doi.org/10.1126/science.279.5349.349
   PubMed Web of Science ®Google Scholar
• Vaziri H, Benchimol S. Reconstitution of telomerase activity in normal human cells leads to elongation of telomeres and extended replicative life span. Curr Biol 1998; 8:279 - 282; PMID: 9501072; http://dx.doi.org/10.1016/S0960-9822(98)70109-5
   PubMed Web of Science ®Google Scholar
• Yan Y, Akhter S, Zhang X, Legerski R. The multifunctional SNM1 gene family: not just nucleases. Future Oncol 2010; 6:1015 - 1029; PMID: 20528238; http://dx.doi.org/10.2217/fon.10.47
   PubMed Web of Science ®Google Scholar
• Beucher A, Birraux J, Tchouandong L, Barton O, Shibata A, Conrad S, et al. ATM and Artemis promote homologous recombination of radiation-induced DNA double-strand breaks in G2. EMBO J 2009; 28:3413 - 3427; PMID: 19779458; http://dx.doi.org/10.1038/emboj.2009.276
   PubMed Web of Science ®Google Scholar
• Fousteri M, Vermeulen W, van Zeeland AA, Mullenders LH. Cockayne syndrome A and B proteins differentially regulate recruitment of chromatin remodeling and repair factors to stalled RNA polymerase II in vivo. Mol Cell 2006; 23:471 - 482; PMID: 16916636; http://dx.doi.org/10.1016/j.molcel.2006.06.029
   PubMed Web of Science ®Google Scholar
• Henning KA, Li L, Iyer N, McDaniel LD, Reagan MS, Legerski R, et al. The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. Cell 1995; 82:555 - 564; PMID: 7664335; http://dx.doi.org/10.1016/0092-8674(95)90028-4
   PubMed Web of Science ®Google Scholar
• Lecanda J, Ganapathy V, D'Aquino-Ardalan C, Evans B, Cadacio C, Ayala A, et al. TGFbeta prevents proteasomal degradation of the cyclin-dependent kinase inhibitor p27kip1 for cell cycle arrest. Cell Cycle 2009; 8:742 - 756; PMID: 19221482; http://dx.doi.org/10.4161/cc.8.5.7871
   PubMed Web of Science ®Google Scholar
• Hara T, Kamura T, Nakayama K, Oshikawa K, Hatakeyama S, Nakayama K. Degradation of p27(Kip1) at the G(0)-G(1) transition mediated by a Skp2-independent ubiquitination pathway. J Biol Chem 2001; 276:48937 - 48943; PMID: 11682478; http://dx.doi.org/10.1074/jbc.M107274200
   PubMed Web of Science ®Google Scholar
• Boehm M, Yoshimoto T, Crook MF, Nallamshetty S, True A, Nabel GJ, et al. A growth factor-dependent nuclear kinase phosphorylates p27(Kip1) and regulates cell cycle progression. EMBO J 2002; 21:3390 - 3401; PMID: 12093740; http://dx.doi.org/10.1093/emboj/cdf343
   PubMed Web of Science ®Google Scholar
• Ganoth D, Bornstein G, Ko TK, Larsen B, Tyers M, Pagano M, et al. The cell cycle regulatory protein Cks1 is required for SCF(Skp2)-mediated ubiquitinylation of p27. Nat Cell Biol 2001; 3:321 - 324; PMID: 11231585; http://dx.doi.org/10.1038/35060126
   PubMed Web of Science ®Google Scholar
• Sitry D, Seeliger MA, Ko TK, Ganoth D, Breward SE, Itzhaki LS, et al. Three different binding sites of Cks1 are required for p27-ubiquitin ligation. J Biol Chem 2002; 277:42233 - 42240; PMID: 12140288; http://dx.doi.org/10.1074/jbc.M205254200
   PubMed Web of Science ®Google Scholar
• Abbas T, Sivaprasad U, Terai K, Amador V, Pagano M, Dutta A. PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex. Genes Dev 2008; 22:2496 - 2506; PMID: 18794347; http://dx.doi.org/10.1101/gad.1676108
   PubMed Web of Science ®Google Scholar
• Rooney S, Sekiguchi J, Zhu C, Cheng HL, Manis J, Whitlow S, et al. Leaky Scid phenotype associated with defective V(D)J coding end processing in Artemis-deficient mice. Mol Cell 2002; 10:1379 - 1390; PMID: 12504013; http://dx.doi.org/10.1016/S1097-2765(02)00755-4
   PubMed Web of Science ®Google Scholar
• Chen X, Zhang Y, Douglas L, Zhou P. UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation. J Biol Chem 2001; 276:48175 - 48182; PMID: 11673459
   PubMed Web of Science ®Google Scholar