RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns

Walden, H. and Rittinger, K. (2018) RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns. Nature Structural and Molecular Biology, 25, pp. 440-445. (doi: 10.1038/s41594-018-0063-3) (PMID:29735995)

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Abstract

RBR ligases are an enigmatic class of E3 ubiquitin ligases that combine properties of RING and HECT-type E3s and undergo multilevel regulation through autoinhibition, post-translational modifications, multimerization and interaction with binding partners. Here, we summarize recent progress in RBR structures and function, which has uncovered commonalities in the mechanisms by which different family members transfer ubiquitin through a multistep process. However, these studies have also highlighted clear differences in the activity of different family members, suggesting that each RBR ligase has evolved specific properties to fit the biological process it regulates.

Item Type:Articles
Additional Information:This work was supported by the Medical Research Council (MRC grant number MC_UU_12016/12) and the European Research Council (ERC-2015-CoG-681582 ICLUb consolidator grant) to H.W. and by the Francis Crick Institute which receives its core funding from Cancer Research UK (FC001142), the UK Medical Research Council (FC001142), and the Wellcome Trust (FC001142) to K.R.
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Walden, Professor Helen
Authors: Walden, H., and Rittinger, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Nature Structural and Molecular Biology
Publisher:Nature Publishing Group
ISSN:1545-9993
ISSN (Online):1545-9985
Published Online:07 May 2018
Copyright Holders:Copyright © 2018 Nature America Inc., part of Springer Nature
First Published:First published in Nature Structural and Molecular Biology 25:440-445
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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