Guard the guardian: A CRL4 ligase stands watch over histone production

References

• Abbas T, Dutta A. CRL4Cdt2: master coordinator of cell cycle progression and genome stability. Cell Cycle 2011; 10:241-9; PMID:21212733; http://dx.doi.org/10.4161/cc.10.2.14530
   PubMed Web of Science ®Google Scholar
• Abbas T, Mueller AC, Shibata E, Keaton M, Rossi M, Dutta A. CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration. Mol Cell 2013; 49:1147-58; PMID:23478445; http://dx.doi.org/10.1016/j.molcel.2013.02.003
   PubMed Web of Science ®Google Scholar
• Abbas T, Shibata E, Park J, Jha S, Karnani N, Dutta A. CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation. Mol Cell 2010; 40:9-21; PMID:20932471; http://dx.doi.org/10.1016/j.molcel.2010.09.014
   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. Gen Dev 2008; 22:2496-506; PMID:18794347; http://dx.doi.org/10.1101/gad.1676108
   PubMed Web of Science ®Google Scholar
• Bond U, Yario TA. The steady state levels and structure of the U7 snRNP are constant during the human cell cycle: lack of cell cycle regulation of histone mRNA 3′ end formation. Cell Mol Biol Res 1994; 40:27-34; PMID:7804324
   PubMedGoogle Scholar
• Bond UM, Yario TA, Steitz JA. Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Gen Dev 1991; 5:1709-22; PMID:1885007; http://dx.doi.org/10.1101/gad.5.9.1709
   PubMed Web of Science ®Google Scholar
• Brodersen MM, Lampert F, Barnes CA, Soste M, Piwko W, Peter M. CRL4(WDR23)-Mediated SLBP Ubiquitylation Ensures Histone Supply during DNA Replication. Mol Cell 2016; 62:627-35; PMID:27203182; http://dx.doi.org/10.1016/j.molcel.2016.04.017
   PubMed Web of Science ®Google Scholar
• Chen W, Moore MJ. The spliceosome: disorder and dynamics defined. Curr Opin Struct Biol 2014; 24:141-9; PMID:24530854; http://dx.doi.org/10.1016/j.sbi.2014.01.009
   PubMed Web of Science ®Google Scholar
• Choi SH, Wright JB, Gerber SA, Cole MD. Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells. Gen Dev 2010; 24:1236-41; PMID:20551172; http://dx.doi.org/10.1101/gad.1920310
   PubMed Web of Science ®Google Scholar
• Dankert JF, Rona G, Clijsters L, Geter P, Skaar JR, Bermudez-Hernandez K, Sassani E, Fenyo D, Ueberheide B, Schneider R, Pagano M. Cyclin F-Mediated Degradation of SLBP Limits H2A.X Accumulation and Apoptosis upon Genotoxic Stress in G2. Mol Cell 2016; 64:507-19; PMID:27773672; http://dx.doi.org/10.1016/j.molcel.2016.09.010
   PubMed Web of Science ®Google Scholar
• Djakbarova U, Marzluff WF, Koseoglu MM. DDB1 and CUL4 associated factor 11 (DCAF11) mediates degradation of Stem-loop binding protein at the end of S phase. Cell cycle 2016; 15:1986-96; PMID:27254819; http://dx.doi.org/10.1080/15384101.2016.1191708
   PubMed Web of Science ®Google Scholar
• Dominski Z, Yang XC, Raska CS, Santiago C, Borchers CH, Duronio RJ, Marzluff WF. 3′ end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system. Mol Cell Biol 2002; 22:6648-60; PMID:12192062; http://dx.doi.org/10.1128/MCB.22.18.6648-6660.2002
   PubMed Web of Science ®Google Scholar
• Dominski Z, Zheng LX, Sanchez R, Marzluff WF. Stem-loop binding protein facilitates 3′-end formation by stabilizing U7 snRNP binding to histone pre-mRNA. Mol Cell Biol 1999; 19:3561-70; PMID:10207079; http://dx.doi.org/10.1128/MCB.19.5.3561
   PubMed Web of Science ®Google Scholar
• Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ. Global identification of modular cullin-RING ligase substrates. Cell 2011; 147:459-74; PMID:21963094; http://dx.doi.org/10.1016/j.cell.2011.09.019
   PubMed Web of Science ®Google Scholar
• Erkmann JA, Sanchez R, Treichel N, Marzluff WF, Kutay U. Nuclear export of metazoan replication-dependent histone mRNAs is dependent on RNA length and is mediated by TAP. Rna 2005; 11:45-58; PMID:15611298; http://dx.doi.org/10.1261/rna.7189205
   PubMed Web of Science ®Google Scholar
• Fischer ES, Scrima A, Bohm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, et al. The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation. Cell 2011; 147:1024-39; PMID:22118460; http://dx.doi.org/10.1016/j.cell.2011.10.035
   PubMed Web of Science ®Google Scholar
• Friend K, Lovejoy AF, Steitz JA. U2 snRNP binds intronless histone pre-mRNAs to facilitate U7-snRNP-dependent 3′ end formation. Mol Cell 2007; 28:240-52; PMID:17964263; http://dx.doi.org/10.1016/j.molcel.2007.09.026
   PubMed Web of Science ®Google Scholar
• Groh BS, Yan F, Smith MD, Yu Y, Chen X, Xiong Y. The antiobesity factor WDTC1 suppresses adipogenesis via the CRL4WDTC1 E3 ligase. EMBO Rep 2016; 17:638-47; PMID:27113764; http://dx.doi.org/10.15252/embr.201540500
   PubMed Web of Science ®Google Scholar
• Han J, Zhang H, Zhang H, Wang Z, Zhou H, Zhang Z. A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly. Cell 2013; 155:817-29; PMID:24209620; http://dx.doi.org/10.1016/j.cell.2013.10.014
   PubMed Web of Science ®Google Scholar
• Harper JW, Bennett EJ. Proteome complexity and the forces that drive proteome imbalance. Nature 2016; 537:328-38; PMID:27629639; http://dx.doi.org/10.1038/nature19947
   PubMed Web of Science ®Google Scholar
• Hart T, Chandrashekhar M, Aregger M, Steinhart Z, Brown KR, MacLeod G, Mis M, Zimmermann M, Fradet-Turcotte A, Sun S, et al. High-Resolution CRISPR Screens Reveal Fitness Genes and Genotype-Specific Cancer Liabilities. Cell 2015; 163:1515-26; PMID:26627737; http://dx.doi.org/10.1016/j.cell.2015.11.015
   PubMed Web of Science ®Google Scholar
• Jaeger S, Barends S, Giege R, Eriani G, Martin F. Expression of metazoan replication-dependent histone genes. Biochimie 2005; 87:827-34; PMID:16164992; http://dx.doi.org/10.1016/j.biochi.2005.03.012
   PubMed Web of Science ®Google Scholar
• Kaygun H, Marzluff WF. Translation termination is involved in histone mRNA degradation when DNA replication is inhibited. Mol Cell Biol 2005; 25:6879-88; PMID:16055702; http://dx.doi.org/10.1128/MCB.25.16.6879-6888.2005
   PubMed Web of Science ®Google Scholar
• Koseoglu MM, Graves LM, Marzluff WF. Phosphorylation of threonine 61 by cyclin a/Cdk1 triggers degradation of stem-loop binding protein at the end of S phase. Mol Cell Biol 2008; 28:4469-79; PMID:18490441; http://dx.doi.org/10.1128/MCB.01416-07
   PubMed Web of Science ®Google Scholar
• Kronke J, Hurst SN, Ebert BL. Lenalidomide induces degradation of IKZF1 and IKZF3. Oncoimmunology 2014a; 3:e941742; PMID:25610725; http://dx.doi.org/10.4161/21624011.2014.941742
   PubMed Web of Science ®Google Scholar
• Kronke J, Udeshi ND, Narla A, Grauman P, Hurst SN, McConkey M, Svinkina T, Heckl D, Comer E, Li X, et al. Lenalidomide causes selective degradation of IKZF1 and IKZF3 in multiple myeloma cells. Science 2014b; 343:301-5; PMID:24292625; http://dx.doi.org/10.1126/science.1244851
   PubMed Web of Science ®Google Scholar
• Lee J, Zhou P. Pathogenic role of the CRL4 ubiquitin ligase in human disease. Front Oncol 2012; 2:21; PMID:22649780
   PubMedGoogle Scholar
• Lee JE, Sweredoski MJ, Graham RL, Kolawa NJ, Smith GT, Hess S, Deshaies RJ. The steady-state repertoire of human SCF ubiquitin ligase complexes does not require ongoing Nedd8 conjugation. Mol Cell Proteomics 2011; 10:M110 006460.
   PubMed Web of Science ®Google Scholar
• Li JM, Jin J. CRL Ubiquitin Ligases and DNA Damage Response. Front Oncol 2012; 2:29; PMID:22655267
   PubMedGoogle Scholar
• Liao H, Liu XJ, Blank JL, Bouck DC, Bernard H, Garcia K, Lightcap ES. Quantitative proteomic analysis of cellular protein modulation upon inhibition of the NEDD8-activating enzyme by MLN4924. Mol Cell Proteomics 2011; 10:M111 009183; http://dx.doi.org/10.1074/mcp.M111.009183
   PubMed Web of Science ®Google Scholar
• Lydeard JR, Schulman BA, Harper JW. Building and remodelling Cullin-RING E3 ubiquitin ligases. EMBO Rep 2013; 14:1050-61; PMID:24232186; http://dx.doi.org/10.1038/embor.2013.173
   PubMed Web of Science ®Google Scholar
• Marzluff WF, Wagner EJ, Duronio RJ. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat Rev Genet 2008; 9:843-54; PMID:18927579; http://dx.doi.org/10.1038/nrg2438
   PubMed Web of Science ®Google Scholar
• Mejlvang J, Feng Y, Alabert C, Neelsen KJ, Jasencakova Z, Zhao X, Lees M, Sandelin A, Pasero P, Lopes M, Groth A. New histone supply regulates replication fork speed and PCNA unloading. J Cell Biol 2014; 204:29-43; PMID:24379417; http://dx.doi.org/10.1083/jcb.201305017
   PubMed Web of Science ®Google Scholar
• Michalski D, Steiniger M. In vivo characterization of the Drosophila mRNA 3′ end processing core cleavage complex. Rna 2015; 21:1404-18; PMID:26081560; http://dx.doi.org/10.1261/rna.049551.115
   PubMed Web of Science ®Google Scholar
• Mouysset J, Gilberto S, Meier MG, Lampert F, Belwal M, Meraldi P, Peter M. CRL4(RBBP7) is required for efficient CENP-A deposition at centromeres. J Cell Sci 2015; 128:1732-45; PMID:25795299; http://dx.doi.org/10.1242/jcs.162305
   PubMed Web of Science ®Google Scholar
• Nakagawa T, Xiong Y. X-linked mental retardation gene CUL4B targets ubiquitylation of H3K4 methyltransferase component WDR5 and regulates neuronal gene expression. Mol Cell 2011; 43:381-91; PMID:21816345; http://dx.doi.org/10.1016/j.molcel.2011.05.033
   PubMed Web of Science ®Google Scholar
• Olma MH, Roy M, Le Bihan T, Sumara I, Maerki S, Larsen B, Quadroni M, Peter M, Tyers M, Pintard L. An interaction network of the mammalian COP9 signalosome identifies Dda1 as a core subunit of multiple Cul4-based E3 ligases. J Cell Sci 2009; 122:1035-44; PMID:19295130; http://dx.doi.org/10.1242/jcs.043539
   PubMed Web of Science ®Google Scholar
• Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005; 6:9-20; PMID:15688063; http://dx.doi.org/10.1038/nrm1547
   PubMed Web of Science ®Google Scholar
• Piwko W, Olma MH, Held M, Bianco JN, Pedrioli PG, Hofmann K, Pasero P, Gerlich DW, Peter M. RNAi-based screening identifies the Mms22L-Nfkbil2 complex as a novel regulator of DNA replication in human cells. EMBO J 2010; 29:4210-22; PMID:21113133; http://dx.doi.org/10.1038/emboj.2010.304
   PubMed Web of Science ®Google Scholar
• Precious B, Childs K, Fitzpatrick-Swallow V, Goodbourn S, Randall RE. Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1. J Virol 2005; 79:13434-41; PMID:16227264; http://dx.doi.org/10.1128/JVI.79.21.13434-13441.2005
   PubMed Web of Science ®Google Scholar
• Sang Y, Yan F, Ren X. The role and mechanism of CRL4 E3 ubiquitin ligase in cancer and its potential therapy implications. Oncotarget 2015; 6:42590-602; PMID:26460955
   PubMed Web of Science ®Google Scholar
• Schaufele F, Gilmartin GM, Bannwarth W, Birnstiel ML. Compensatory mutations suggest that base-pairing with a small nuclear RNA is required to form the 3′ end of H3 messenger RNA. Nature 1986; 323:777-81; PMID:3022153; http://dx.doi.org/10.1038/323777a0
   PubMed Web of Science ®Google Scholar
• Scrima A, Konickova R, Czyzewski BK, Kawasaki Y, Jeffrey PD, Groisman R, Nakatani Y, Iwai S, Pavletich NP, Thoma NH. Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell 2008; 135:1213-23; PMID:19109893; http://dx.doi.org/10.1016/j.cell.2008.10.045
   PubMed Web of Science ®Google Scholar
• Su C, Gao G, Schneider S, Helt C, Weiss C, O'Reilly MA, Bohmann D, Zhao J. DNA damage induces downregulation of histone gene expression through the G1 checkpoint pathway. EMBO J 2004; 23:1133-43; PMID:14976556; http://dx.doi.org/10.1038/sj.emboj.7600120
   PubMed Web of Science ®Google Scholar
• Sullivan KD, Mullen TE, Marzluff WF, Wagner EJ. Knockdown of SLBP results in nuclear retention of histone mRNA. Rna 2009; 15:459-72; PMID:19155325; http://dx.doi.org/10.1261/rna.1205409
   PubMed Web of Science ®Google Scholar
• Tan D, Marzluff WF, Dominski Z, Tong L. Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3′hExo ternary complex. Science 2013; 339:318-21; PMID:23329046; http://dx.doi.org/10.1126/science.1228705
   PubMed Web of Science ®Google Scholar
• Teixeira LK, Reed SI. Ubiquitin ligases and cell cycle control. Ann Rev Biochem 2013; 82:387-414; PMID:23495935; http://dx.doi.org/10.1146/annurev-biochem-060410-105307
   PubMed Web of Science ®Google Scholar
• Terai K, Abbas T, Jazaeri AA, Dutta A. CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis. Mol Cell 2010; 37:143-9; PMID:20129063; http://dx.doi.org/10.1016/j.molcel.2009.12.018
   PubMed Web of Science ®Google Scholar
• Vasserot AP, Schaufele FJ, Birnstiel ML. Conserved terminal hairpin sequences of histone mRNA precursors are not involved in duplex formation with the U7 RNA but act as a target site for a distinct processing factor. Proc Natl Acad Sci U S A 1989; 86:4345-9; PMID:2734288; http://dx.doi.org/10.1073/pnas.86.12.4345
   PubMed Web of Science ®Google Scholar
• Wang Z, Dai X, Zhong J, Inuzuka H, Wan L, Li X, Wang L, Ye X, Sun L, Gao D, et al. SCF(beta-TRCP) promotes cell growth by targeting PR-Set7/Set8 for degradation. Nat Commun 2015; 6:10185; PMID:26666832; http://dx.doi.org/10.1038/ncomms10185
   PubMed Web of Science ®Google Scholar
• Yau R, Rape M. The increasing complexity of the ubiquitin code. Nat Cell Biol 2016; 18:579-86; PMID:27230526; http://dx.doi.org/10.1038/ncb3358
   PubMed Web of Science ®Google Scholar
• Zeman MK, Cimprich KA. Causes and consequences of replication stress. Nat Cell Biol 2014; 16:2-9; PMID:24366029; http://dx.doi.org/10.1038/ncb2897
   PubMed Web of Science ®Google Scholar
• Zeng M, Ren L, Mizuno K, Nestoras K, Wang H, Tang Z, Guo L, Kong D, Hu Q, He Q, et al. CRL4(Wdr70) regulates H2B monoubiquitination and facilitates Exo1-dependent resection. Nat Commun 2016; 7:11364; PMID:27098497; http://dx.doi.org/10.1038/ncomms11364
   PubMed Web of Science ®Google Scholar
• Zhang J, Tan D, DeRose EF, Perera L, Dominski Z, Marzluff WF, Tong L, Hall TM. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation. Proc Natl Acad Sci U S A 2014; 111:E2937-2946; PMID:25002523; http://dx.doi.org/10.1073/pnas.1406381111
   PubMed Web of Science ®Google Scholar
• Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization. Biochemistry 2012; 51:3215-31; PMID:22439849; http://dx.doi.org/10.1021/bi2018255
   PubMed Web of Science ®Google Scholar
• Zheng L, Dominski Z, Yang XC, Elms P, Raska CS, Borchers CH, Marzluff WF. Phosphorylation of stem-loop binding protein (SLBP) on 2 threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase. Mol Cell Biol 2003; 23:1590-601; PMID:12588979; http://dx.doi.org/10.1128/MCB.23.5.1590-1601.2003
   PubMed Web of Science ®Google Scholar