Abstract
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.
Document Type
Review
Publication Date
8-27-2018
Digital Object Identifier (DOI)
https://doi.org/10.3390/cells7090118
Funding Information
Our research was supported by the Shared Resources of the University of Kentucky Markey Cancer Center (P30CA177558). Our research was also supported by grants from American Cancer Society Research Scholar Award (RSG13187) and NIH (P20GM121327 and CA230758) to Yadi Wu.
Repository Citation
Wang, Jianlin; Qiu, Zhaoping; and Wu, Yadi, "Ubiquitin Regulation: The Histone Modifying Enzyme's Story" (2018). Pharmacology and Nutritional Sciences Faculty Publications. 75.
https://uknowledge.uky.edu/pharmacol_facpub/75
Included in
Cell and Developmental Biology Commons, Enzymes and Coenzymes Commons, Genetics and Genomics Commons
Notes/Citation Information
Published in Cells, v. 7, issue 9, 118, p. 1-19.
© 2018 by the authors. Licensee MDPI, Basel, Switzerland.
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).