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 |
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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 > School of Molecular Biosciences |
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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