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Kuo AJ, Cheung P, Chen K, Zee BM, Kioi M, Lauring J, Xi Y, Park BH, Shi X, Garcia BA, Li W, Gozani O (2011) NSD2 links dimethylation of histone H3 at lysine 36 to oncogenic programming. Guttman M, Amit I, Garber M, French C, Lin MF, Feldser D, Huarte M, Zuk O, Carey BW, Cassady JP, Cabili MN, Jaenisch R, Mikkelsen TS, Jacks T, Hacohen N, Bernstein BE, Kellis M, Regev A, Rinn JL, Lander ES (2009) Chromatin signature reveals over a thousand highly conserved large non-coding RNAs in mammals. Mikkelsen TS, Ku M, Jaffe DB, Issac B, Lieberman E, Giannoukos G, Alvarez P, Brockman W, Kim TK, Koche RP, Lee W, Mendenhall E, OРІР‚в„ўDonovan A, Presser A, Russ C, Xie X, Meissner A, Wernig M, Jaenisch R, Nusbaum C, Lander ES, Bernstein BE (2007) Genome-wide maps of chromatin state in pluripotent and lineage-committed cells. Yuan W, Xu M, Huang C, Liu N, Chen S, Zhu B (2011) H3K36 methylation antagonizes PRC2-mediated H3K27 methylation. Xu B, On DM, Ma A, Parton T, Konze KD, Pattenden SG, Allison DF, Cai L, Rockowitz S, Liu S, Liu Y, Li F, Vedadi M, Frye SV, Garcia BA, Zheng D, Jin J, Wang GG (2015) Selective inhibition of EZH2 and EZH1 enzymatic activity by a small molecule suppresses MLL-rearranged leukemia. J Proteome Res 15:1070РІР‚вЂњ1079Р”В«hanu NV, Sidoli S, Garcia BA (2016) Histone modification profiling reveals differential signatures associated with human embryonic stem cell self-renewal and differentiation. Yu Y, Chen J, Gao Y, Gao J, Liao R, Wang Y, Oyang C, Li E, Zeng C, Zhou S, Yang P, Jin H, Yi W (2016) Quantitative profiling of combinational K27/K36 modifications on histone H3 variants in mouse organs. Zheng Y, Sweet SM, Popovic R, Martinez-Garcia E, Tipton JD, Thomas PM, Licht JD, Kelleher NL (2012) Total kinetic analysis reveals how combinatorial methylation patterns are established on lysines 27 and 36 of histone H3. Cell 128:693РІР‚вЂњ705Р”В¬hi P, Allis CD, Wang GG (2010) Covalent histone modifications-miswritten, misinterpreted and mis-erased in human cancers. Kouzarides T (2007) Chromatin modifications and their function. Huang H, Sabari BR, Garcia BA, Allis CD, Zhao Y (2014) SnapShot: histone modifications. Henikoff S, Smith MM (2015) Histone variants and epigenetics. Strahl BD, Allis CD (2000) The language of covalent histone modifications. This review will elaborate on current advances in understanding H3K36 methylation and related molecular players during various chromatin-templated cellular processes, their crosstalks with other chromatin factors, as well as their deregulations in the diseased contexts. Additionally, recurrent mutations of H3K36 and surrounding histone residues are detected in human tumors, further highlighting the importance of H3K36 in biology and medicine. Deregulation of H3K36 methylation and related regulatory factors leads to pathogenesis of disease such as developmental syndrome and cancer. These H3K36 methylation-mediated events are biologically crucial and controlled by different classes of proteins responsible for either РІР‚ВwritingРІР‚в„ў, РІР‚ВreadingРІР‚в„ў or РІР‚ВerasingРІР‚в„ў of H3K36 methylation marks. Trimethylation of H3K36 (H3K36me3) demarcates body regions of the actively transcribed genes, providing signals for modulating transcription fidelity, mRNA splicing and DNA damage repair and di-methylation of H3K36 (H3K36me2) spreads out within large intragenic regions, regulating distribution of histone H3 lysine 27 trimethylation (H3K27me3) and possibly DNA methylation. Methylation of histone H3 lysine 36 (H3K36) plays crucial roles in the partitioning of chromatin to distinctive domains and the regulation of a wide range of biological processes.

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