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Updated: Feb 10, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
RBR ligase-mediated ubiquitin transfer: a tale with many twists and turns
Helen Walden1, Katrin Rittinger2
1Institute of Molecular Cell and Systems Biology, University of Glasgow, Glasgow, Scotland, UK. Helen.Walden@glasgow.ac.uk.
Abstract:
RBR ligases are an enigmatic class of E3 ubiquitin ligases that combine properties of RING and HECT-type E3s and undergo multilevel regulation through autoinhibition, post-translational modifications, multimerization and interaction with binding partners. Here, we summarize recent progress in RBR structures and function, which has uncovered commonalities in the mechanisms by which different family members transfer ubiquitin through a multistep process. However, these studies have also highlighted clear differences in the activity of different family members, suggesting that each RBR ligase has evolved specific properties to fit the biological process it regulates.
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