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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Faculty of 1000 Ltd
2013
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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. |
format | Online Article Text |
id | pubmed-3816760 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Faculty of 1000 Ltd |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT yangxiangjiao sumoylationingeneregulationhumandiseaseandtherapeuticaction AT chiangchengming sumoylationingeneregulationhumandiseaseandtherapeuticaction |