Structure, location, function, and regulation of SUMO specific protease family

doi:11.3969/j.issn.1674-8115.2014.11.025

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Structure, location, function, and regulation of SUMO specific protease family

MIAO Yu¹, ZHAO Wen-bo¹, LI Qing², YI Jing³, HAN Yan²

1.Basic Medicine Faculty of Shanghai Jiao Tong University, Shanghai 200025, China; 2.Department of Infectious Diseases, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China; 3.Department of Biochemistry and Molecular Cell Biology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China

Online:2014-11-28 Published:2014-12-02
Supported by:
National Natural Science Foundation of China, 81302086; Special Scientific Research Foundation for University Doctorate of China, 20130073120007; Type A Project of Shanghai Pujiang Program of Shanghai Scientific and Technological Talents Project, 13PJ1406100

Abstract

Abstract:

Post-translational modification of proteins plays a very important role in regulating function, activity and positioning of proteins, as well as the progression of cell cycle and cell differentiation. SUMOylation (SUMO, small ubiquitin-like modifier) is a highly dynamic process which can be reserved by SUMO specific proteases (SENPs) family. SENPs can catalyze and remove SUMO from SUMO-connecting target proteins, as well as from their precursor proteins. Furthermore, some members of this family are involved in the maturation and activation of SUMO. Thus, deSUMOylation is as important as SUMOylation to the regulation of function and activity of SUMO-connecting proteins. This paper reviews the structure and biological characteristics of SENPs family.

Key words: SUMOylation, deSUMOylation, SUMO specific protease, Ulp, Ulp domain

MIAO Yu, ZHAO Wen-bo, LI Qing, et al. Structure, location, function, and regulation of SUMO specific protease family[J]. , doi: 11.3969/j.issn.1674-8115.2014.11.025.

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Structure, location, function, and regulation of SUMO specific protease family

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