Taking Me away: the function of phosphorylation on histone lysine demethylases

Trends Biochem Sci. 2024 Jan 16:S0968-0004(23)00299-2. doi: 10.1016/j.tibs.2023.12.004. Online ahead of print.ABSTRACTHistone 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.PMID:38233282 | DOI:10.1016/j.tibs.2023.12.004

Source: Trends in Biochemical Sciences - January 17, 2024 Category: Biochemistry Authors: Nicola M Karakatsanis Joshua J Hamey Marc R Wilkins Source Type: research