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

Autor: Karakatsanis NM; Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, UNSW, Sydney, Australia., Hamey JJ; Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, UNSW, Sydney, Australia., Wilkins MR; Systems Biology Initiative, School of Biotechnology and Biomolecular Sciences, UNSW, Sydney, Australia. Electronic address: m.wilkins@unsw.edu.au.
Jazyk: angličtina
Zdroj: Trends in biochemical sciences [Trends Biochem Sci] 2024 Mar; Vol. 49 (3), pp. 257-276. Date of Electronic Publication: 2024 Jan 16.
DOI: 10.1016/j.tibs.2023.12.004
Abstrakt: 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.
Competing Interests: Declaration of interests The authors declare no competing interests.
(Copyright © 2023 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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