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Ubiquitin Regulation: The Histone Modifying Enzyme′s Story

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. Intere...

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Detalles Bibliográficos
Autores principales: Wang, Jianlin, Qiu, Zhaoping, Wu, Yadi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162602/
https://www.ncbi.nlm.nih.gov/pubmed/30150556
http://dx.doi.org/10.3390/cells7090118
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author Wang, Jianlin
Qiu, Zhaoping
Wu, Yadi
author_facet Wang, Jianlin
Qiu, Zhaoping
Wu, Yadi
author_sort Wang, Jianlin
collection PubMed
description 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.
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spelling pubmed-61626022018-10-02 Ubiquitin Regulation: The Histone Modifying Enzyme′s Story Wang, Jianlin Qiu, Zhaoping Wu, Yadi Cells Review 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. MDPI 2018-08-27 /pmc/articles/PMC6162602/ /pubmed/30150556 http://dx.doi.org/10.3390/cells7090118 Text en © 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/).
spellingShingle Review
Wang, Jianlin
Qiu, Zhaoping
Wu, Yadi
Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title_full Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title_fullStr Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title_full_unstemmed Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title_short Ubiquitin Regulation: The Histone Modifying Enzyme′s Story
title_sort ubiquitin regulation: the histone modifying enzyme′s story
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162602/
https://www.ncbi.nlm.nih.gov/pubmed/30150556
http://dx.doi.org/10.3390/cells7090118
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