Structural insights into the catalysis and regulation of E3 ubiquitin ligases

Buetow, L. and Huang, D. T. (2016) Structural insights into the catalysis and regulation of E3 ubiquitin ligases. Nature Reviews Molecular Cell Biology, 17(10), pp. 626-642. (doi: 10.1038/nrm.2016.91) (PMID:27485899)

Abstract

Covalent attachment (conjugation) of one or more ubiquitin molecules to protein substrates governs numerous eukaryotic cellular processes, including apoptosis, cell division and immune responses. Ubiquitylation was originally associated with protein degradation, but it is now clear that ubiquitylation also mediates processes such as protein–protein interactions and cell signalling depending on the type of ubiquitin conjugation. Ubiquitin ligases (E3s) catalyse the final step of ubiquitin conjugation by transferring ubiquitin from ubiquitin-conjugating enzymes (E2s) to substrates. In humans, more than 600 E3s contribute to determining the fates of thousands of substrates; hence, E3s need to be tightly regulated to ensure accurate substrate ubiquitylation. Recent findings illustrate how E3s function on a structural level and how they coordinate with E2s and substrates to meticulously conjugate ubiquitin. Insights regarding the mechanisms of E3 regulation, including structural aspects of their autoinhibition and activation are also emerging.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Huang, Professor Danny and Buetow, Dr Lori
• Authors: Buetow, L., and Huang, D. T.
• College/School: College of Medical Veterinary and Life Sciences > School of Cancer Sciences
• Journal Name: Nature Reviews Molecular Cell Biology
• Publisher: Nature Publishing Group
• ISSN: 1471-0072
• ISSN (Online): 1471-0080
• Published Online: 03 August 2016
• Copyright Holders: Copyright © 2016 Nature Publishing Group
• First Published: First published in Nature Reviews Molecular Cell Biology 17(10):626-642
• Publisher Policy: Reproduced in accordance with the copyright policy of the publisher