Histone 4 lysine 20 tri-methylation: a key epigenetic regulator in chromatin structure and disease

Alejandra Agredo; Andrea L Kasinski

doi:10.3389/fgene.2023.1243395

Histone 4 lysine 20 tri-methylation: a key epigenetic regulator in chromatin structure and disease

Front Genet. 2023 Aug 21:14:1243395. doi: 10.3389/fgene.2023.1243395. eCollection 2023.

Authors

Alejandra Agredo^{1

2}, Andrea L Kasinski^{1

3}

Affiliations

¹ Department of Biological Sciences, Purdue University, West Lafayette, IN, United States.
² Purdue Life Sciences Interdisciplinary Program (PULSe), Purdue University, West Lafayette, IN, United States.
³ Purdue Institute for Cancer Research, Purdue University, West Lafayette, IN, United States.

Abstract

Chromatin is a vital and dynamic structure that is carefully regulated to maintain proper cell homeostasis. A great deal of this regulation is dependent on histone proteins which have the ability to be dynamically modified on their tails via various post-translational modifications (PTMs). While multiple histone PTMs are studied and often work in concert to facilitate gene expression, here we focus on the tri-methylation of histone H4 on lysine 20 (H4K20me3) and its function in chromatin structure, cell cycle, DNA repair, and development. The recent studies evaluated in this review have shed light on how H4K20me3 is established and regulated by various interacting partners and how H4K20me3 and the proteins that interact with this PTM are involved in various diseases. Through analyzing the current literature on H4K20me3 function and regulation, we aim to summarize this knowledge and highlights gaps that remain in the field.

Keywords: H4K20me3; cancer; chromatin; disease; heterochromatin; histone; homeostasis; methylation.

Publication types

Review

Grants and funding

This study was funded in part by the National Institutes of Health (R01CA205420 and R01CA226259) to AK, a LCRP Idea Development Award from the Department of Defense (W81XWH-22-1-1085) to AK, and a grant from the NIH to the Purdue Institute for Cancer Research (P30CA023168). AA was supported by a SIRG grant from the Purdue Institute for Cancer Research and a Ross Lynn Fellowship from Purdue University.