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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...

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Autores principales: Yang, Yanfang, He, Yu, Wang, Xixi, liang, Ziwei, He, Gu, Zhang, Peng, Zhu, Hongxia, Xu, Ningzhi, Liang, Shufang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2017
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.
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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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