Karakatsanis Nicola M, Hamey Joshua J, Wilkins Marc R
Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, UNSW, Sydney, Australia.
Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, UNSW, Sydney, Australia.
Trends Biochem Sci. 2024 Mar;49(3):257-276. doi: 10.1016/j.tibs.2023.12.004. Epub 2024 Jan 16.
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.
组蛋白赖氨酸去甲基化酶（KDMs）通过催化从组蛋白中去除甲基基团来调节真核基因转录。这些酶受到激酶信号系统的复杂调控，以响应内部和外部刺激。在这里，我们综述激酶介导的磷酸化影响人类组蛋白KDM功能的机制。这些机制包括改变组蛋白KDM的亚细胞定位或与染色质的结合、改变蛋白质半衰期、导致组蛋白去甲基化、非组蛋白去甲基化或去甲基酶非依赖性效应的组蛋白KDM复合物形成的变化，以及对组蛋白KDM复合物解离的影响。我们还探讨了组蛋白KDM上磷酸化位点的结构背景，并评估其与功能的关系。
