Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3

Alpi, A. F., Chaugule, V. and Walden, H. (2016) Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3. Biochemical Journal, 473(20), pp. 3401-3419. (doi: 10.1042/BCJ20160028) (PMID:27729585) (PMCID:PMC5095918)

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Ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. Many disease states are associated with dysfunction of ubiquitin signalling, with the E3s being a particular focus. However, recent evidence demonstrates that mutations or impairment of the E2s can lead to severe disease states, including chromosome instability syndromes, cancer predisposition, and immunological disorders. Given their relevance to diseases, E2s may represent an important class of therapeutic targets. In the present study, we review the current understanding of the mechanism of this important family of enzymes, and the role of selected E2s in disease.

Item Type:Articles
Additional Information:This work was funded by Cancer Research UK (17739) (to H.W. and V.C.), the Medical Research Council (MC_UU_1206/12), a grant from the Scottish Government to The Scottish Institute for Cell Signalling (A.F.A.), and the EMBO Young Investigator Programme (H.W.)
Glasgow Author(s) Enlighten ID:Chaugule, Dr Viduth and Walden, Professor Helen
Authors: Alpi, A. F., Chaugule, V., and Walden, H.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Biochemical Journal
Publisher:Portland Press Ltd.
ISSN (Online):1470-8728
Published Online:11 October 2016
Copyright Holders:Copyright © 2016 The Authors
First Published:First published in Biochemical Journal 473(20):3401-3419
Publisher Policy:Reproduced under a Creative Commons License

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