Protein SUMOylation modification and its associations with disease

• Published in: Open biology Vol. 7; no. 10; p. 170167
• Main Authors: Yang, Yanfang, He, Yu, Wang, Xixi, liang, Ziwei, He, Gu, Zhang, Peng, Zhu, Hongxia, Xu, Ningzhi, Liang, Shufang
• Format: Journal Article
• Language: English
• Published: England The Royal Society 01-10-2017
• Subjects: Animals; Desumoylation; Disease; Disease Susceptibility; Humans; Protein Processing, Post-Translational; Proteins - genetics; Proteins - metabolism; Review; Signal Transduction; Sumo Pathway; Sumoylation; Ubiquitin - metabolism; Ubiquitination; SUMO pathway; disease; SUMOylation; deSUMOylation
• ISSN: 2046-2441; 2046-2441
• DOI: 10.1098/rsob.170167

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.