The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family

Xiangyi S. Wang; Thomas R. Cotton; Sarah J. Trevelyan; Lachlan W. Richardson; Wei Ting Lee; John Silke; Bernhard C. Lechtenberg

doi:10.1038/s41467-023-35871-z

Nature Communications (Jan 2023)

The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase family

Xiangyi S. Wang,
Thomas R. Cotton,
Sarah J. Trevelyan,
Lachlan W. Richardson,
Wei Ting Lee,
John Silke,
Bernhard C. Lechtenberg

Affiliations

Xiangyi S. Wang: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
Thomas R. Cotton: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
Sarah J. Trevelyan: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
Lachlan W. Richardson: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
Wei Ting Lee: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
John Silke: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research
Bernhard C. Lechtenberg: Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research

DOI: https://doi.org/10.1038/s41467-023-35871-z
Journal volume & issue: Vol. 14, no. 1
pp. 1 – 17

Abstract

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RBR E3 ubiquitin ligases utilise a 2-step catalytic mechanism previously defined for only few of the RBR family members. Here, the authors examine the poorly studied RBRs HOIL-1 and RNF216 to define general principles of RBR catalysis and regulation and identify specific functional differences.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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