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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2018
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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. |
format | Online Article Text |
id | pubmed-6162602 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT wangjianlin ubiquitinregulationthehistonemodifyingenzymesstory AT qiuzhaoping ubiquitinregulationthehistonemodifyingenzymesstory AT wuyadi ubiquitinregulationthehistonemodifyingenzymesstory |