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Sumoylation in gene regulation, human disease, and therapeutic action

Similar to ubiquitination, sumoylation covalently attaches a small ubiquitin-like modifier (SUMO) protein (92–97 amino acids) to the ε-amino group of a lysine residue. This is quite different from the classically defined post-translational modifications, such as phosphorylation, acetylation, and met...

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Autores principales: Yang, Xiang-Jiao, Chiang, Cheng-Ming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Faculty of 1000 Ltd 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3816760/
https://www.ncbi.nlm.nih.gov/pubmed/24273646
http://dx.doi.org/10.12703/P5-45
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author Yang, Xiang-Jiao
Chiang, Cheng-Ming
author_facet Yang, Xiang-Jiao
Chiang, Cheng-Ming
author_sort Yang, Xiang-Jiao
collection PubMed
description Similar to ubiquitination, sumoylation covalently attaches a small ubiquitin-like modifier (SUMO) protein (92–97 amino acids) to the ε-amino group of a lysine residue. This is quite different from the classically defined post-translational modifications, such as phosphorylation, acetylation, and methylation, which typically add a small chemical group to the targeted residue. Sumoylation has been well studied at the molecular and cellular levels, focusing mostly on site-specific conjugation of human SUMO1, SUMO2, and SUMO3, as well as their homologues in various species. In this short review, we will discuss some recent examples to highlight (a) emerging trends about the coordinated regulation of sumoylation and other post-translational modifications in modulating the function of some transcription factors and pathway-specific regulators, (b) diverse roles of sumoylation in gene regulation implicated in stem cells and different pathogenic conditions, and (c) potential therapeutic strategies related to some of the diseases stated above.
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spelling pubmed-38167602013-11-22 Sumoylation in gene regulation, human disease, and therapeutic action Yang, Xiang-Jiao Chiang, Cheng-Ming F1000Prime Rep Review Article Similar to ubiquitination, sumoylation covalently attaches a small ubiquitin-like modifier (SUMO) protein (92–97 amino acids) to the ε-amino group of a lysine residue. This is quite different from the classically defined post-translational modifications, such as phosphorylation, acetylation, and methylation, which typically add a small chemical group to the targeted residue. Sumoylation has been well studied at the molecular and cellular levels, focusing mostly on site-specific conjugation of human SUMO1, SUMO2, and SUMO3, as well as their homologues in various species. In this short review, we will discuss some recent examples to highlight (a) emerging trends about the coordinated regulation of sumoylation and other post-translational modifications in modulating the function of some transcription factors and pathway-specific regulators, (b) diverse roles of sumoylation in gene regulation implicated in stem cells and different pathogenic conditions, and (c) potential therapeutic strategies related to some of the diseases stated above. Faculty of 1000 Ltd 2013-11-01 /pmc/articles/PMC3816760/ /pubmed/24273646 http://dx.doi.org/10.12703/P5-45 Text en © 2013 Faculty of 1000 Ltd http://creativecommons.org/licenses/by-nc/3.0/legalcode This is an open-access article distributed under the terms of the Creative Commons Attribution-Non Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. You may not use this work for commercial purposes
spellingShingle Review Article
Yang, Xiang-Jiao
Chiang, Cheng-Ming
Sumoylation in gene regulation, human disease, and therapeutic action
title Sumoylation in gene regulation, human disease, and therapeutic action
title_full Sumoylation in gene regulation, human disease, and therapeutic action
title_fullStr Sumoylation in gene regulation, human disease, and therapeutic action
title_full_unstemmed Sumoylation in gene regulation, human disease, and therapeutic action
title_short Sumoylation in gene regulation, human disease, and therapeutic action
title_sort sumoylation in gene regulation, human disease, and therapeutic action
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3816760/
https://www.ncbi.nlm.nih.gov/pubmed/24273646
http://dx.doi.org/10.12703/P5-45
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