Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination

Gundogdu, M. and Walden, H. (2019) Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination. Protein Science, 28(10), pp. 1758-1770. (doi: 10.1002/pro.3690) (PMID:31340062)

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Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cascade of ubiquitin activating (E1), conjugating (E2) and ligating (E3) enzymes assemble distinct ubiquitin signals on target proteins. E2s specify the type of ubiquitin signal generated, while E3s associate with the E2~Ub conjugate and select the substrate for ubiquitination. Thus, producing the right ubiquitin signal on the right target requires the right E2-E3 pair. The question of how over 600 E3s evolved to discriminate between 38 structurally related E2s has therefore been an area of intensive research, and with over 50 E2-E3 complex structures generated to date, the answer is beginning to emerge. The following review discusses the structural basis of generic E2-RING E3 interactions, contrasted with emerging themes that reveal how specificity can be achieved.

Item Type:Articles
Keywords:E2, E2-E3 specificity, RING E3, structural basis of specificity, ubiquitination.
Glasgow Author(s) Enlighten ID:Gundogdu, Dr Mehmet and Walden, Professor Helen
Authors: Gundogdu, M., and Walden, H.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Protein Science
ISSN (Online):1469-896X
Published Online:24 July 2019
Copyright Holders:Copyright © 2019 The Protein Society
First Published:First published in Protein Science 28(10):1758-1770
Publisher Policy:Reproduced in accordance with the publisher copyright policy

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