期刊
EPIGENETICS
卷 13, 期 7, 页码 683-692出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15592294.2018.1503491
关键词
Histone; H3K36M; cancer; PTM; methylation
资金
- National Institute of General Medical Sciences [GM106416, GM101664, GM100907, GM126900]
- NATIONAL CANCER INSTITUTE [P30CA016086] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM106416, R01GM100907, R01GM101664] Funding Source: NIH RePORTER
Histone posttranslational modifications control the organization and function of chromatin. In particular, methylation of lysine 36 in histone H3 (H3K36me) has been shown to mediate gene transcription, DNA repair, cell cycle regulation, and pre-mRNA splicing. Notably, mutations at or near this residue have been causally linked to the development of several human cancers. These observations have helped to illuminate the role of histones themselves in disease and to clarify the mechanisms by which they acquire oncogenic properties. This perspective focuses on recent advances in discovery and characterization of histone H3 mutations that impact H3K36 methylation. We also highlight findings that the common cancer-related substitution of H3K36 to methionine (H3K36M) disturbs functions of not only H3K36me-writing enzymes but also H3K36me-specific readers. The latter case suggests that the oncogenic effects could also be linked to the inability of readers to engage H3K36M.
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