组蛋白甲基转移酶
组蛋白甲基化
组蛋白H2A
组蛋白密码
组蛋白H1
组蛋白八聚体
脱甲基酶
SAP30型
组蛋白
组蛋白脱乙酰基酶2
生物
细胞生物学
组蛋白脱乙酰基酶5
生物化学
组蛋白H3
化学
核小体
DNA甲基化
基因表达
基因
组蛋白脱乙酰基酶
作者
Nicola M. Karakatsanis,Joshua J. Hamey,Marc R. Wilkins
标识
DOI:10.1016/j.tibs.2023.12.004
摘要
Abstract
Histone lysine demethylases (KDMs) regulate eukaryotic gene transcription by catalysing the removal of methyl groups from histone proteins. These enzymes are intricately regulated by the kinase signalling system in response to internal and external stimuli. Here, we review the mechanisms by which kinase-mediated phosphorylation influence human histone KDM function. These include the changing of histone KDM subcellular localisation or chromatin binding, the altering of protein half-life, changes to histone KDM complex formation that result in histone demethylation, non-histone demethylation or demethylase-independent effects, and effects on histone KDM complex dissociation. We also explore the structural context of phospho-sites on histone KDMs and evaluate how this relates to function.
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