Journal
NATURE REVIEWS MOLECULAR CELL BIOLOGY
Volume 18, Issue 2, Pages 90-101Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm.2016.140
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Funding
- Rockefeller University
- US National Cancer Institute [CA204639]
- US National Institutes of Health (NIH) [GM105933, DK107868, GM115961]
- US National Science Foundation (NSF) Graduate Research Fellowship Program [DGE-1325261]
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Eight types of short-chain Lys acylations have recently been identified on histones: propionylation, butyrylation, 2-hydroxyisobutyrylation, succinylation, malonylation, glutarylation, crotonylation and beta-hydroxybutyrylation. Emerging evidence suggests that these histone modifications affect gene expression and are structurally and functionally different from the widely studied histone Lys acetylation. In this Review, we discuss the regulation of non-acetyl histone acylation by enzymatic and metabolic mechanisms, the acylation 'reader' proteins that mediate the effects of different acylations and their physiological functions, which include signal-dependent gene activation, spermatogenesis, tissue injury and metabolic stress. We propose a model to explain our present understanding of how differential histone acylation is regulated by the metabolism of the different acyl-CoA forms, which in turn modulates the regulation of gene expression.
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