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Ubiquitin Regulation: The Histone Modifying Enzyme′s Story

by Jianlin Wang 1,2, Zhaoping Qiu 1,2 and Yadi Wu 1,2,*
1
Department of Pharmacology & Nutritional Sciences, University of Kentucky School of Medicine, KY 40506, USA
2
Markey Cancer Center, University of Kentucky School of Medicine, Lexington, KY 40506, USA
*
Author to whom correspondence should be addressed.
Cells 2018, 7(9), 118; https://doi.org/10.3390/cells7090118
Received: 26 July 2018 / Revised: 22 August 2018 / Accepted: 23 August 2018 / Published: 27 August 2018
(This article belongs to the Special Issue Ubiquitination in Health and Disease)
Histone post-translational modifications influence many fundamental cellular events by regulating chromatin structure and gene transcriptional activity. These modifications are highly dynamic and tightly controlled, with many enzymes devoted to the addition and removal of these modifications. Interestingly, these modifying enzymes are themselves fine-tuned and precisely regulated at the level of protein turnover by ubiquitin-proteasomal processing. Here, we focus on recent progress centered on the mechanisms regulating ubiquitination of histone modifying enzymes, including ubiquitin proteasomal degradation and the reverse process of deubiquitination. We will also discuss the potential pathophysiological significance of these processes. View Full-Text
Keywords: ubiquitin; epigenetic; histone modifying enzyme; protein degradation ubiquitin; epigenetic; histone modifying enzyme; protein degradation
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MDPI and ACS Style

Wang, J.; Qiu, Z.; Wu, Y. Ubiquitin Regulation: The Histone Modifying Enzyme′s Story. Cells 2018, 7, 118.

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