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Updated: May 5, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
Published on: January 29, 2018
Sumoylation in gene regulation, human disease, and therapeutic action
Xiang-Jiao Yang1, Cheng-Ming Chiang
1The Rosalind & Morris Goodman Cancer Research Center, McGill University Montréal, Québec, H3A 1A3 Canada ; Department of Medicine, McGill University Montréal, Québec, H3A 1A3 Canada.
Abstract:
Similar to ubiquitination, sumoylation covalently attaches a small ubiquitin-like modifier (SUMO) protein (92-97 amino acids) to the ε-amino group of a lysine residue. This is quite different from the classically defined post-translational modifications, such as phosphorylation, acetylation, and methylation, which typically add a small chemical group to the targeted residue. Sumoylation has been well studied at the molecular and cellular levels, focusing mostly on site-specific conjugation of human SUMO1, SUMO2, and SUMO3, as well as their homologues in various species. In this short review, we will discuss some recent examples to highlight (a) emerging trends about the coordinated regulation of sumoylation and other post-translational modifications in modulating the function of some transcription factors and pathway-specific regulators, (b) diverse roles of sumoylation in gene regulation implicated in stem cells and different pathogenic conditions, and (c) potential therapeutic strategies related to some of the diseases stated above.
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