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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Main Authors: Yanfang Yang, Yu He, Xixi Wang, Ziwei liang, Gu He, Peng Zhang, Hongxia Zhu, Ningzhi Xu, Shufang Liang
Format: Article
Language:English
Published: The Royal Society 2017-01-01
Series:Open Biology
Subjects:
Online Access:https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170167
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spelling doaj-00c1f9d2d7a746b3b1076b6fff38c6a82020-11-25T03:00:08ZengThe Royal SocietyOpen Biology2046-24412017-01-0171010.1098/rsob.170167170167Protein SUMOylation modification and its associations with diseaseYanfang YangYu HeXixi WangZiwei liangGu HePeng ZhangHongxia ZhuNingzhi XuShufang LiangSUMOylation, 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.https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170167sumoylationsumo pathwaydesumoylationdisease
collection DOAJ
language English
format Article
sources DOAJ
author Yanfang Yang
Yu He
Xixi Wang
Ziwei liang
Gu He
Peng Zhang
Hongxia Zhu
Ningzhi Xu
Shufang Liang
spellingShingle Yanfang Yang
Yu He
Xixi Wang
Ziwei liang
Gu He
Peng Zhang
Hongxia Zhu
Ningzhi Xu
Shufang Liang
Protein SUMOylation modification and its associations with disease
Open Biology
sumoylation
sumo pathway
desumoylation
disease
author_facet Yanfang Yang
Yu He
Xixi Wang
Ziwei liang
Gu He
Peng Zhang
Hongxia Zhu
Ningzhi Xu
Shufang Liang
author_sort Yanfang Yang
title Protein SUMOylation modification and its associations with disease
title_short 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_sort protein sumoylation modification and its associations with disease
publisher The Royal Society
series Open Biology
issn 2046-2441
publishDate 2017-01-01
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.
topic sumoylation
sumo pathway
desumoylation
disease
url https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.170167
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