Modes of allosteric regulation of the ubiquitination machinery

Rennie, M. L. , Chaugule, V. K. and Walden, H. (2020) Modes of allosteric regulation of the ubiquitination machinery. Current Opinion in Structural Biology, 62, pp. 189-196. (doi: 10.1016/j.sbi.2020.02.003) (PMID:32305021)

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Abstract

Ubiquitination is a post-translational modification crucial for cellular signaling. A diverse range of enzymes constitute the machinery that mediates attachment of ubiquitin onto target proteins. This diversity allows the targeting of various proteins in a highly regulated fashion. Many of the enzymes have multiple domains or subunits that bind allosteric effectors and exhibit large conformational rearrangements to facilitate regulation. Here we consider recent examples of ubiquitin itself as an allosteric effector of RING and RBR E3 ligases, as well as advances in the understanding of allosteric regulatory elements within HECT E3 ligases.

Item Type:Articles
Additional Information:This work was supported by the EMBO Young Investigator Programme to H.W.; the European Research Council (ERC-2015-CoG-681582 ICLUb) consolidator grant to H.W.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Chaugule, Dr Viduth and Rennie, Dr Martin and Walden, Professor Helen
Authors: Rennie, M. L., Chaugule, V. K., and Walden, H.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Current Opinion in Structural Biology
Publisher:Elsevier
ISSN:0959-440X
ISSN (Online):1879-033X
Published Online:15 April 2020
Copyright Holders:Copyright © 2020 Elsevier Ltd.
First Published:First published in Current Opinion in Structural Biology 62:189-196
Publisher Policy:Reproduced in accordance with the publisher copyright policy

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