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Review
. 2017 Oct;7(10):170167.
doi: 10.1098/rsob.170167.

Protein SUMOylation modification and its associations with disease

Yanfang Yang  1 , Yu He  1 , Xixi Wang  1 , Ziwei Liang  1 , Gu He  1 , Peng Zhang  2 , Hongxia Zhu  3 , Ningzhi Xu  1   3 , Shufang Liang  4
Affiliations
Review

Protein SUMOylation modification and its associations with disease

Yanfang Yang et al. Open Biol. 2017 Oct.

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.

Keywords: SUMO pathway; SUMOylation; deSUMOylation; disease.

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Conflict of interest statement

All authors declare no conflict of interest.

Figures

Figure 1.
Figure 1.
Biochemical process of SUMO modifications in mammal cells. All small ubiquitin-like modifier (SUMO) paralogues are synthesized as pre-proteins that are first cleaved by a SENP to expose a carboxy-terminal diglycine (GG) motif (maturation). An ATP-requiring activation step by the heterodimeric E1activating enzyme (including SAE1 and SAE2) then generates a SUMO–SAE2 thioester. SUMO is then transferred to the E2 conjugating enzyme Ubc9, again forming a thioester. This last step usually requires a SUMO E3 ligase to bring about an isopeptide bond between the SUMO C-terminus and a lysine within the target protein.
Figure 2.
Figure 2.
Relationship of SUMO-modified proteins with different diseases, along with some examples of representative proteins and SUMO pathway members.
Figure 3.
Figure 3.
Several methods to identify SUMOylation site. SUMO modification sites are predicted using bioinformatics software analysis. The prediction site is verified using the following methods. (a) The SUMOylation site is analysed through site-directed mutagenesis and Co-IP. (b) SUMO modification site is identified by mass spectrometry.
See this image and copyright information in PMC

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