Protein SUMOylation modification and its associations with disease

Author:

Yang Yanfang1ORCID,He Yu1,Wang Xixi1,liang Ziwei1,He Gu1,Zhang Peng2,Zhu Hongxia3,Xu Ningzhi13,Liang Shufang1

Affiliation:

1. State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, No.17, 3rd Section of People's South Road, Chengdu, 610041, People's Republic of China

2. Department of Urinary Surgery, West China Hospital, Sichuan University, Chengdu, 610041, Sichuan, People's Republic of China

3. Laboratory of Cell and Molecular Biology & State Key Laboratory of Molecular Oncology, Cancer Institute & Cancer Hospital, Chinese Academy of Medical Sciences, Beijing, 100034, People's Republic of China

Abstract

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.

Funder

National Key Basic Research Program of China

National Natural Science Foundation of China

cience and Technology Department of Sichuan Province

Health and Family Planning Commission of Sichuan Province

Publisher

The Royal Society

Subject

General Biochemistry, Genetics and Molecular Biology,Immunology,General Neuroscience

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