Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs

Histone lysine methyltransferases (HKMTs) are key regulators of many cellular processes. By definition, HKMTs catalyse the methylation of lysine residues in histone proteins. The enzymatic activities of HKMTs are under precise control, with their allosteric regulation emerging as a prevalent paradig...

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Detalles Bibliográficos
Autores principales: Davidovich, Chen, Zhang, Qi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2021
Materias:
Review Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8106495/
https://www.ncbi.nlm.nih.gov/pubmed/33769454
http://dx.doi.org/10.1042/BST20200238
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author Davidovich, Chen
Zhang, Qi
author_facet Davidovich, Chen
Zhang, Qi
author_sort Davidovich, Chen
collection PubMed
description Histone lysine methyltransferases (HKMTs) are key regulators of many cellular processes. By definition, HKMTs catalyse the methylation of lysine residues in histone proteins. The enzymatic activities of HKMTs are under precise control, with their allosteric regulation emerging as a prevalent paradigm. We review the molecular mechanisms of allosteric regulation of HKMTs using well-studied histone H3 (K4, K9, K27 and K36) methyltransferases as examples. We discuss the current advances and future potential in targeting allosteric sites of HKMTs for drug development.
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spelling pubmed-81064952021-05-18 Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs Davidovich, Chen Zhang, Qi Biochem Soc Trans Review Articles Histone lysine methyltransferases (HKMTs) are key regulators of many cellular processes. By definition, HKMTs catalyse the methylation of lysine residues in histone proteins. The enzymatic activities of HKMTs are under precise control, with their allosteric regulation emerging as a prevalent paradigm. We review the molecular mechanisms of allosteric regulation of HKMTs using well-studied histone H3 (K4, K9, K27 and K36) methyltransferases as examples. We discuss the current advances and future potential in targeting allosteric sites of HKMTs for drug development. Portland Press Ltd. 2021-04-30 2021-03-26 /pmc/articles/PMC8106495/ /pubmed/33769454 http://dx.doi.org/10.1042/BST20200238 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0/) . Open access for this article was enabled by the participation of Monash University in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with CAUL.
spellingShingle Review Articles
Davidovich, Chen
Zhang, Qi
Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title_full Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title_fullStr Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title_full_unstemmed Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title_short Allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
title_sort allosteric regulation of histone lysine methyltransferases: from context-specific regulation to selective drugs
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8106495/
https://www.ncbi.nlm.nih.gov/pubmed/33769454
http://dx.doi.org/10.1042/BST20200238
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