Metabolic regulation of gene expression through histone acylations
By Benjamin R. Sabari, Di Zhang, C. D. Allis, Yingming Zhao. Nature reviews. Molecular cell biology, 2016
943 citations recorded by the source corpus.
Eight types of short-chain Lys acylations have recently been identified on histones: propionylation, butyrylation, 2-hydroxyisobutyrylation, succinylation, malonylation, glutarylation, crotonylation and β-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.
Subfields: Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/8baf7f7dbef28284608a4228c0d54d35ebb15a15
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Citations in the corpus
- Class I histone deacetylases (HDAC1–3) are histone lysine delactylases (2021, background): “Therefore, like acetyl-CoA and histone lysine acetylation (Kac) (14), histone K(L-la) represents another example showing that acyl-CoA species can affect gene expression directly via histone posttranslational modification (PTM).”
- Histone lactylation drives oncogenesis by facilitating m6A reader protein YTHDF2 expression in ocular melanoma (2021, background): “tone acylation marks derived from cellular metabolites were newly discovered, such as propionylation, butyrylation, succinylation, and malonylation [10].”
- Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “Three major families of KATs, GNAT (G protein subunit alpha transducin), MYST (Moz, Ybf2/Sas3, Sas2, and Tip60), and p300/CBP (E1Abinding protein p300/CREB-binding protein), have been identified (Sabari et al., 2017).”
- Histone Marks in the 'Driver's Seat': Functional Roles in Steering the Transcription Cycle. (2017, background): “In addition to histone lysine acetylation, it is becoming more appreciated that additional acyl short chain modifications are common histone modifications [7] and may also play critical roles in transcription (reviewed in [51]).”