A lesson learned from the H3.3K27M mutation found in pediatric glioma

References

• Schwartzentruber J, Korshunov A, Liu XY, Jones DT, Pfaff E, Jacob K, et al. Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma. Nature 2012; 482:226 - 31; http://dx.doi.org/10.1038/nature10833; PMID: 22286061
   PubMed Web of Science ®Google Scholar
• Wu G, Broniscer A, McEachron TA, Lu C, Paugh BS, Becksfort J, et al, St. Jude Children’s Research Hospital–Washington University Pediatric Cancer Genome Project. Somatic histone H3 alterations in pediatric diffuse intrinsic pontine gliomas and non-brainstem glioblastomas. Nat Genet 2012; 44:251 - 3; http://dx.doi.org/10.1038/ng.1102; PMID: 22286216
   PubMed Web of Science ®Google Scholar
• Sturm D, Witt H, Hovestadt V, Khuong-Quang DA, Jones DT, Konermann C, et al. Hotspot mutations in H3F3A and IDH1 define distinct epigenetic and biological subgroups of glioblastoma. Cancer Cell 2012; 22:425 - 37; http://dx.doi.org/10.1016/j.ccr.2012.08.024; PMID: 23079654
   PubMed Web of Science ®Google Scholar
• Chan KM, Fang D, Gan H, Hashizume R, Yu C, Schroeder M, et al. The histone H3.3K27M mutation in pediatric glioma reprograms H3K27 methylation and gene expression. Genes Dev 2013; 27:985 - 90; http://dx.doi.org/10.1101/gad.217778.113; PMID: 23603901
   PubMed Web of Science ®Google Scholar
• Lewis PW, Müller MM, Koletsky MS, Cordero F, Lin S, Banaszynski LA, et al. Inhibition of PRC2 activity by a gain-of-function H3 mutation found in pediatric glioblastoma. Science 2013; 340:857 - 61; http://dx.doi.org/10.1126/science.1232245; PMID: 23539183
   PubMed Web of Science ®Google Scholar
• Elsässer SJ, Allis CD, Lewis PW. Cancer. New epigenetic drivers of cancers. Science 2011; 331:1145 - 6; http://dx.doi.org/10.1126/science.1203280; PMID: 21385704
   PubMed Web of Science ®Google Scholar
• You JS, Jones PA. Cancer genetics and epigenetics: two sides of the same coin?. Cancer Cell 2012; 22:9 - 20; http://dx.doi.org/10.1016/j.ccr.2012.06.008; PMID: 22789535
   PubMed Web of Science ®Google Scholar
• Swami M. Epigenetics: Demethylation links cell fate and cancer. Nat Rev Genet 2010; 11:749; http://dx.doi.org/10.1038/nrg2890; PMID: 20921960
   PubMed Web of Science ®Google Scholar
• Rodríguez-Paredes M, Esteller M. Cancer epigenetics reaches mainstream oncology. Nat Med 2011; 17:330 - 9; http://dx.doi.org/10.1038/nm.2305; PMID: 21386836
   PubMed Web of Science ®Google Scholar
• Lund AH, van Lohuizen M. Epigenetics and cancer. Genes Dev 2004; 18:2315 - 35; http://dx.doi.org/10.1101/gad.1232504; PMID: 15466484
   PubMed Web of Science ®Google Scholar
• Rice JC, Ozcelik H, Maxeiner P, Andrulis I, Futscher BW. Methylation of the BRCA1 promoter is associated with decreased BRCA1 mRNA levels in clinical breast cancer specimens. Carcinogenesis 2000; 21:1761 - 5; http://dx.doi.org/10.1093/carcin/21.9.1761; PMID: 10964110
   PubMed Web of Science ®Google Scholar
• Rice JC, Futscher BW. Transcriptional repression of BRCA1 by aberrant cytosine methylation, histone hypoacetylation and chromatin condensation of the BRCA1 promoter. Nucleic Acids Res 2000; 28:3233 - 9; http://dx.doi.org/10.1093/nar/28.17.3233; PMID: 10954590
   PubMed Web of Science ®Google Scholar
• Tapia T, Smalley SV, Kohen P, Muñoz A, Solis LM, Corvalan A, et al. Promoter hypermethylation of BRCA1 correlates with absence of expression in hereditary breast cancer tumors. Epigenetics 2008; 3:157 - 63; http://dx.doi.org/10.4161/epi.3.3.6387; PMID: 18567944
   PubMed Web of Science ®Google Scholar
• Smith E, Lin C, Shilatifard A. The super elongation complex (SEC) and MLL in development and disease. Genes Dev 2011; 25:661 - 72; http://dx.doi.org/10.1101/gad.2015411; PMID: 21460034
   PubMed Web of Science ®Google Scholar
• Mohan M, Lin C, Guest E, Shilatifard A. Licensed to elongate: a molecular mechanism for MLL-based leukaemogenesis. Nat Rev Cancer 2010; 10:721 - 8; http://dx.doi.org/10.1038/nrc2915; PMID: 20844554
   PubMed Web of Science ®Google Scholar
• McCabe MT, Graves AP, Ganji G, Diaz E, Halsey WS, Jiang Y, et al. Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27). Proc Natl Acad Sci U S A 2012; 109:2989 - 94; http://dx.doi.org/10.1073/pnas.1116418109; PMID: 22323599
   PubMed Web of Science ®Google Scholar
• Morin RD, Johnson NA, Severson TM, Mungall AJ, An J, Goya R, et al. Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin. Nat Genet 2010; 42:181 - 5; http://dx.doi.org/10.1038/ng.518; PMID: 20081860
   PubMed Web of Science ®Google Scholar
• Béguelin W, Popovic R, Teater M, Jiang Y, Bunting KL, Rosen M, et al. EZH2 is required for germinal center formation and somatic EZH2 mutations promote lymphoid transformation. Cancer Cell 2013; 23:677 - 92; http://dx.doi.org/10.1016/j.ccr.2013.04.011; PMID: 23680150
   PubMed Web of Science ®Google Scholar
• Ahmad K, Henikoff S. Histone H3 variants specify modes of chromatin assembly. Proc Natl Acad Sci U S A 2002; 99:Suppl 4 16477 - 84; http://dx.doi.org/10.1073/pnas.172403699; PMID: 12177448
   PubMed Web of Science ®Google Scholar
• Ahmad K, Henikoff S. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol Cell 2002; 9:1191 - 200; http://dx.doi.org/10.1016/S1097-2765(02)00542-7; PMID: 12086617
   PubMed Web of Science ®Google Scholar
• Szenker E, Ray-Gallet D, Almouzni G. The double face of the histone variant H3.3. Cell Res 2011; 21:421 - 34; http://dx.doi.org/10.1038/cr.2011.14; PMID: 21263457
   PubMed Web of Science ®Google Scholar
• Khuong-Quang DA, Buczkowicz P, Rakopoulos P, Liu XY, Fontebasso AM, Bouffet E, et al. K27M mutation in histone H3.3 defines clinically and biologically distinct subgroups of pediatric diffuse intrinsic pontine gliomas. Acta Neuropathol 2012; 124:439 - 47; http://dx.doi.org/10.1007/s00401-012-0998-0; PMID: 22661320
   PubMed Web of Science ®Google Scholar
• Steiner LA, Schulz VP, Maksimova Y, Wong C, Gallagher PG. Patterns of histone H3 lysine 27 monomethylation and erythroid cell type-specific gene expression. J Biol Chem 2011; 286:39457 - 65; http://dx.doi.org/10.1074/jbc.M111.243006; PMID: 21937433
   PubMed Web of Science ®Google Scholar
• Plath K, Fang J, Mlynarczyk-Evans SK, Cao R, Worringer KA, Wang H, et al. Role of histone H3 lysine 27 methylation in X inactivation. Science 2003; 300:131 - 5; http://dx.doi.org/10.1126/science.1084274; PMID: 12649488
   PubMed Web of Science ®Google Scholar
• Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002; 298:1039 - 43; http://dx.doi.org/10.1126/science.1076997; PMID: 12351676
   PubMed Web of Science ®Google Scholar
• Margueron R, Reinberg D. The Polycomb complex PRC2 and its mark in life. Nature 2011; 469:343 - 9; http://dx.doi.org/10.1038/nature09784; PMID: 21248841
   PubMed Web of Science ®Google Scholar
• Creyghton MP, Cheng AW, Welstead GG, Kooistra T, Carey BW, Steine EJ, et al. Histone H3K27ac separates active from poised enhancers and predicts developmental state. Proc Natl Acad Sci U S A 2010; 107:21931 - 6; http://dx.doi.org/10.1073/pnas.1016071107; PMID: 21106759
   PubMed Web of Science ®Google Scholar
• Heintzman ND, Hon GC, Hawkins RD, Kheradpour P, Stark A, Harp LF, et al. Histone modifications at human enhancers reflect global cell-type-specific gene expression. Nature 2009; 459:108 - 12; http://dx.doi.org/10.1038/nature07829; PMID: 19295514
   PubMed Web of Science ®Google Scholar
• Hashizume R, Smirnov I, Liu S, Phillips JJ, Hyer J, McKnight TR, et al. Characterization of a diffuse intrinsic pontine glioma cell line: implications for future investigations and treatment. J Neurooncol 2012; 110:305 - 13; http://dx.doi.org/10.1007/s11060-012-0973-6; PMID: 22983601
   PubMed Web of Science ®Google Scholar
• Panning B, Dausman J, Jaenisch R. X chromosome inactivation is mediated by Xist RNA stabilization. Cell 1997; 90:907 - 16; http://dx.doi.org/10.1016/S0092-8674(00)80355-4; PMID: 9298902
   PubMed Web of Science ®Google Scholar
• Lee JT, Jaenisch R. The (epi)genetic control of mammalian X-chromosome inactivation. Curr Opin Genet Dev 1997; 7:274 - 80; http://dx.doi.org/10.1016/S0959-437X(97)80138-4; PMID: 9115428
   PubMed Web of Science ®Google Scholar
• Lyon MF. Gene action in the X-chromosome of the mouse (Mus musculus L.). Nature 1961; 190:372 - 3; http://dx.doi.org/10.1038/190372a0; PMID: 13764598
   PubMed Web of Science ®Google Scholar
• Chow J, Heard E. X inactivation and the complexities of silencing a sex chromosome. Curr Opin Cell Biol 2009; 21:359 - 66; http://dx.doi.org/10.1016/j.ceb.2009.04.012; PMID: 19477626
   PubMed Web of Science ®Google Scholar
• Kidder BL, Hu G, Zhao K. ChIP-Seq: technical considerations for obtaining high-quality data. Nat Immunol 2011; 12:918 - 22; http://dx.doi.org/10.1038/ni.2117; PMID: 21934668
   PubMed Web of Science ®Google Scholar
• McCabe MT, Ott HM, Ganji G, Korenchuk S, Thompson C, Van Aller GS, et al. EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature 2012; 492:108 - 12; http://dx.doi.org/10.1038/nature11606; PMID: 23051747
   PubMed Web of Science ®Google Scholar
• Qi W, Chan H, Teng L, Li L, Chuai S, Zhang R, et al. Selective inhibition of Ezh2 by a small molecule inhibitor blocks tumor cells proliferation. Proc Natl Acad Sci U S A 2012; 109:21360 - 5; http://dx.doi.org/10.1073/pnas.1210371110; PMID: 23236167
   PubMed Web of Science ®Google Scholar
• Agger K, Cloos PA, Christensen J, Pasini D, Rose S, Rappsilber J, et al. UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 2007; 449:731 - 4; http://dx.doi.org/10.1038/nature06145; PMID: 17713478
   PubMed Web of Science ®Google Scholar
• Hong S, Cho YW, Yu LR, Yu H, Veenstra TD, Ge K. Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Proc Natl Acad Sci U S A 2007; 104:18439 - 44; http://dx.doi.org/10.1073/pnas.0707292104; PMID: 18003914
   PubMed Web of Science ®Google Scholar
• Miller SA, Mohn SE, Weinmann AS. Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression. Mol Cell 2010; 40:594 - 605; http://dx.doi.org/10.1016/j.molcel.2010.10.028; PMID: 21095589
   PubMed Web of Science ®Google Scholar
• Kruidenier L, Chung CW, Cheng Z, Liddle J, Che K, Joberty G, et al. A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response. Nature 2012; 488:404 - 8; http://dx.doi.org/10.1038/nature11262; PMID: 22842901
   PubMed Web of Science ®Google Scholar
• Nguyen AT, Zhang Y. The diverse functions of Dot1 and H3K79 methylation. Genes Dev 2011; 25:1345 - 58; http://dx.doi.org/10.1101/gad.2057811; PMID: 21724828
   PubMed Web of Science ®Google Scholar
• Frederiks F, Tzouros M, Oudgenoeg G, van Welsem T, Fornerod M, Krijgsveld J, et al. Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states. Nat Struct Mol Biol 2008; 15:550 - 7; http://dx.doi.org/10.1038/nsmb.1432; PMID: 18511943
   PubMed Web of Science ®Google Scholar
• Wysocka J, Allis CD, Coonrod S. Histone arginine methylation and its dynamic regulation. Front Biosci 2006; 11:344 - 55; http://dx.doi.org/10.2741/1802; PMID: 16146736
   PubMed Web of Science ®Google Scholar
• Wang Y, Wysocka J, Sayegh J, Lee YH, Perlin JR, Leonelli L, et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 2004; 306:279 - 83; http://dx.doi.org/10.1126/science.1101400; PMID: 15345777
   PubMed Web of Science ®Google Scholar
• Torres-Padilla ME, Parfitt DE, Kouzarides T, Zernicka-Goetz M. Histone arginine methylation regulates pluripotency in the early mouse embryo. Nature 2007; 445:214 - 8; http://dx.doi.org/10.1038/nature05458; PMID: 17215844
   PubMed Web of Science ®Google Scholar
• Kirmizis A, Santos-Rosa H, Penkett CJ, Singer MA, Vermeulen M, Mann M, et al. Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation. Nature 2007; 449:928 - 32; http://dx.doi.org/10.1038/nature06160; PMID: 17898715
   PubMed Web of Science ®Google Scholar
• Zippo A, De Robertis A, Serafini R, Oliviero S. PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation. Nat Cell Biol 2007; 9:932 - 44; http://dx.doi.org/10.1038/ncb1618; PMID: 17643117
   PubMed Web of Science ®Google Scholar
• Lau AT, Lee SY, Xu YM, Zheng D, Cho YY, Zhu F, et al. Phosphorylation of histone H2B serine 32 is linked to cell transformation. J Biol Chem 2011; 286:26628 - 37; http://dx.doi.org/10.1074/jbc.M110.215590; PMID: 21646345
   PubMed Web of Science ®Google Scholar
• Kang B, Pu M, Hu G, Wen W, Dong Z, Zhao K, et al. Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly. Genes Dev 2011; 25:1359 - 64; http://dx.doi.org/10.1101/gad.2055511; PMID: 21724829
   PubMed Web of Science ®Google Scholar
• Zhang Y. Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev 2003; 17:2733 - 40; http://dx.doi.org/10.1101/gad.1156403; PMID: 14630937
   PubMed Web of Science ®Google Scholar
• Zhang F, Yu X. WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription. Mol Cell 2011; 41:384 - 97; http://dx.doi.org/10.1016/j.molcel.2011.01.024; PMID: 21329877
   PubMed Web of Science ®Google Scholar
• Barski A, Cuddapah S, Cui K, Roh TY, Schones DE, Wang Z, et al. High-resolution profiling of histone methylations in the human genome. Cell 2007; 129:823 - 37; http://dx.doi.org/10.1016/j.cell.2007.05.009; PMID: 17512414
   PubMed Web of Science ®Google Scholar
• Bernstein BE, Mikkelsen TS, Xie X, Kamal M, Huebert DJ, Cuff J, et al. A bivalent chromatin structure marks key developmental genes in embryonic stem cells. Cell 2006; 125:315 - 26; http://dx.doi.org/10.1016/j.cell.2006.02.041; PMID: 16630819
   PubMed Web of Science ®Google Scholar
• Dunham I, Kundaje A, Aldred SF, Collins PJ, Davis CA, Doyle F, et al, ENCODE Project Consortium. An integrated encyclopedia of DNA elements in the human genome. Nature 2012; 489:57 - 74; http://dx.doi.org/10.1038/nature11247; PMID: 22955616
   PubMed Web of Science ®Google Scholar
• Burgess RJ, Zhou H, Han J, Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol Cell 2010; 37:469 - 80; http://dx.doi.org/10.1016/j.molcel.2010.01.020; PMID: 20188666
   PubMed Web of Science ®Google Scholar
• Li Q, Fazly AM, Zhou H, Huang S, Zhang Z, Stillman B. The elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents. PLoS Genet 2009; 5:e1000684; http://dx.doi.org/10.1371/journal.pgen.1000684; PMID: 19834596
   PubMed Web of Science ®Google Scholar
• Li Q, Zhou H, Wurtele H, Davies B, Horazdovsky B, Verreault A, et al. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 2008; 134:244 - 55; http://dx.doi.org/10.1016/j.cell.2008.06.018; PMID: 18662540
   PubMed Web of Science ®Google Scholar
• Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM, Zhang Z. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 2007; 315:653 - 5; http://dx.doi.org/10.1126/science.1133234; PMID: 17272723
   PubMed Web of Science ®Google Scholar
• Dang W, Steffen KK, Perry R, Dorsey JA, Johnson FB, Shilatifard A, et al. Histone H4 lysine 16 acetylation regulates cellular lifespan. Nature 2009; 459:802 - 7; http://dx.doi.org/10.1038/nature08085; PMID: 19516333
   PubMed Web of Science ®Google Scholar
• Nakanishi S, Sanderson BW, Delventhal KM, Bradford WD, Staehling-Hampton K, Shilatifard A. A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation. Nat Struct Mol Biol 2008; 15:881 - 8; http://dx.doi.org/10.1038/nsmb.1454; PMID: 18622391
   PubMed Web of Science ®Google Scholar
• Yuan J, Pu M, Zhang Z, Lou Z. Histone H3-K56 acetylation is important for genomic stability in mammals. Cell Cycle 2009; 8:1747 - 53; http://dx.doi.org/10.4161/cc.8.11.8620; PMID: 19411844
   PubMed Web of Science ®Google Scholar
• Pengelly AR, Copur O, Jäckle H, Herzig A, Müller J. A histone mutant reproduces the phenotype caused by loss of histone-modifying factor Polycomb. Science 2013; 339:698 - 9; http://dx.doi.org/10.1126/science.1231382; PMID: 23393264
   PubMed Web of Science ®Google Scholar
• Henikoff S, Ahmad K. Assembly of variant histones into chromatin. Annu Rev Cell Dev Biol 2005; 21:133 - 53; http://dx.doi.org/10.1146/annurev.cellbio.21.012704.133518; PMID: 16212490
   PubMed Web of Science ®Google Scholar
• Ui-Tei K, Naito Y, Nishi K, Juni A, Saigo K. Thermodynamic stability and Watson-Crick base pairing in the seed duplex are major determinants of the efficiency of the siRNA-based off-target effect. Nucleic Acids Res 2008; 36:7100 - 9; http://dx.doi.org/10.1093/nar/gkn902; PMID: 18988625
   PubMed Web of Science ®Google Scholar
• Lee JM, Lee JS, Kim H, Kim K, Park H, Kim JY, et al. EZH2 generates a methyl degron that is recognized by the DCAF1/DDB1/CUL4 E3 ubiquitin ligase complex. Mol Cell 2012; 48:572 - 86; http://dx.doi.org/10.1016/j.molcel.2012.09.004; PMID: 23063525
   PubMed Web of Science ®Google Scholar
• Li F, Mao G, Tong D, Huang J, Gu L, Yang W, et al. The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSα. Cell 2013; 153:590 - 600; http://dx.doi.org/10.1016/j.cell.2013.03.025; PMID: 23622243
   PubMed Web of Science ®Google Scholar
• Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J, et al. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 2006; 127:1361 - 73; http://dx.doi.org/10.1016/j.cell.2006.10.043; PMID: 17190600
   PubMed Web of Science ®Google Scholar
• Chan KM, Zhang H, Malureanu L, van Deursen J, Zhang Z. Diverse factors are involved in maintaining X chromosome inactivation. Proc Natl Acad Sci U S A 2011; 108:16699 - 704; http://dx.doi.org/10.1073/pnas.1107616108; PMID: 21940502
   PubMed Web of Science ®Google Scholar
• Chan KM, Zhang Z. Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing. J Biol Chem 2012; 287:15024 - 33; http://dx.doi.org/10.1074/jbc.M111.337980; PMID: 22427655
   PubMed Web of Science ®Google Scholar