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Protein SUMOylation modification and its associations with disease
SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5666083/ https://www.ncbi.nlm.nih.gov/pubmed/29021212 http://dx.doi.org/10.1098/rsob.170167 |
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author | Yang, Yanfang He, Yu Wang, Xixi liang, Ziwei He, Gu Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang |
author_facet | Yang, Yanfang He, Yu Wang, Xixi liang, Ziwei He, Gu Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang |
author_sort | Yang, Yanfang |
collection | PubMed |
description | SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site. With the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease. |
format | Online Article Text |
id | pubmed-5666083 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-56660832017-11-15 Protein SUMOylation modification and its associations with disease Yang, Yanfang He, Yu Wang, Xixi liang, Ziwei He, Gu Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang Open Biol Review SUMOylation, as a post-translational modification, plays essential roles in various biological functions including cell growth, migration, cellular responses to stress and tumorigenesis. The imbalance of SUMOylation and deSUMOylation has been associated with the occurrence and progression of various diseases. Herein, we summarize and discuss the signal crosstalk between SUMOylation and ubiquitination of proteins, protein SUMOylation relations with several diseases, and the identification approaches for SUMOylation site. With the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease. The Royal Society 2017-10-11 /pmc/articles/PMC5666083/ /pubmed/29021212 http://dx.doi.org/10.1098/rsob.170167 Text en © 2017 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited. |
spellingShingle | Review Yang, Yanfang He, Yu Wang, Xixi liang, Ziwei He, Gu Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang Protein SUMOylation modification and its associations with disease |
title | Protein SUMOylation modification and its associations with disease |
title_full | Protein SUMOylation modification and its associations with disease |
title_fullStr | Protein SUMOylation modification and its associations with disease |
title_full_unstemmed | Protein SUMOylation modification and its associations with disease |
title_short | Protein SUMOylation modification and its associations with disease |
title_sort | protein sumoylation modification and its associations with disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5666083/ https://www.ncbi.nlm.nih.gov/pubmed/29021212 http://dx.doi.org/10.1098/rsob.170167 |
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