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Taking Me away: the function of phosphorylation on histone lysine demethylases
Trends in Biochemical Sciences ( IF 13.8 ) Pub Date : 2024-01-16 , DOI: 10.1016/j.tibs.2023.12.004
Nicola M. Karakatsanis , Joshua J. Hamey , Marc R. Wilkins

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.

中文翻译:

带我走:磷酸化对组蛋白赖氨酸脱甲基酶的作用

组蛋白赖氨酸去甲基酶 (KDM) 通过催化去除组蛋白中的甲基来调节真核基因转录。这些酶受到激酶信号系统的复杂调节,以响应内部和外部刺激。在这里,我们回顾了激酶介导的磷酸化影响人类组蛋白 KDM 功能的机制。这些包括组蛋白 KDM 亚细胞定位或染色质结合的变化、蛋白质半衰期的改变、导致组蛋白去甲基化、非组蛋白去甲基化或去甲基化酶独立效应的组蛋白 KDM 复合物形成的变化,以及对组蛋白 KDM 复合物解离的影响。我们还探索了组蛋白 KDM 上磷酸位点的结构背景,并评估其与功能的关系。
更新日期:2024-01-16
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