Specificity and disease in the ubiquitin system

Chaugule, V. K. and Walden, H. (2016) Specificity and disease in the ubiquitin system. Biochemical Society Transactions, 44(1), pp. 212-227. (doi: 10.1042/BST20150209) (PMID:26862208) (PMCID:PMC5264512)

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Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality control and degradation pathways. A huge range of ubiquitin signals can be generated depending on the specificity and catalytic activity of the enzymes required for attachment of ubiquitin to a given target. As a consequence of its importance to eukaryotic life, dysfunction in the ubiquitin system leads to many disease states, including cancers and neurodegeneration. This review takes a retrospective look at our progress in understanding the molecular mechanisms that govern the specificity of ubiquitin conjugation.

Item Type:Articles
Additional Information:This work was supported by the Cancer Research UK [grant number 17739]; the Medical Research Council [grant number MC_UU_12016/12]; and the EMBO Young Investigator Programme.
Glasgow Author(s) Enlighten ID:Chaugule, Dr Viduth and Walden, Professor Helen
Authors: Chaugule, V. K., and Walden, H.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Biochemical Society Transactions
Publisher:Portland Press Ltd.
ISSN (Online):1470-8752
Published Online:09 February 2016
Copyright Holders:Copyright © 2016 The Authors
First Published:First published in Biochemical Society Transactions 44(1):212-227
Publisher Policy:Reproduced under a Creative Commons License

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