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Updated: Jul 8, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
Published on: January 29, 2018
Highly sensitive assays for SUMOylation and small ubiquitin-like modifier-dependent protein-protein interactions
Nathalie Rouleau1, Jianghai Wang, Labrini Karras
1PerkinElmer BioSignal, Montreal, Quebec H3J 1R4, Canada. nathalie.rouleau@perkinelmer.com
Abstract:
Small ubiquitin-like proteins (SUMO) are recently discovered post-translational modifiers that regulate protein functions and intracellular trafficking. In this study, we are describing two chemoluminescence-based assays, one for SUMOylation and another one for SUMO-mediated protein-protein interactions. These assays can be used to characterize the activity and kinetics of the enzymes that catalyze SUMOylation, and in high-throughput screening for inhibitors of SUMOylation and SUMO-dependent protein-protein interactions. These novel assays represent the most sensitive assays for ubiquitin-like systems published to date. Similar strategies can be used to develop assays for other ubiquitin-like modification systems.
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