Chain reactions: molecular mechanisms of RBR ubiquitin ligases.
| Autor: | Cotton TR; Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia.; Department of Medical Biology, The University of Melbourne, Parkville, VIC 3010, Australia., Lechtenberg BC; Ubiquitin Signalling Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, VIC 3052, Australia.; Department of Medical Biology, The University of Melbourne, Parkville, VIC 3010, Australia. |
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| Jazyk: | angličtina |
| Zdroj: | Biochemical Society transactions [Biochem Soc Trans] 2020 Aug 28; Vol. 48 (4), pp. 1737-1750. |
| DOI: | 10.1042/BST20200237 |
| Abstrakt: | Ubiquitination is a fundamental post-translational modification that regulates almost all aspects of cellular signalling and is ultimately catalysed by the action of E3 ubiquitin ligases. The RING-between-RING (RBR) family of E3 ligases encompasses 14 distinct human enzymes that are defined by a unique domain organisation and catalytic mechanism. Detailed characterisation of several RBR ligase family members in the last decade has revealed common structural and mechanistic features. At the same time these studies have highlighted critical differences with respect to autoinhibition, activation and catalysis. Importantly, the majority of RBR E3 ligases remain poorly studied, and thus the extent of diversity within the family remains unknown. In this mini-review we outline the current understanding of the RBR E3 mechanism, structure and regulation with a particular focus on recent findings and developments that will shape the field in coming years. (© 2020 The Author(s).) |
| Databáze: | MEDLINE |
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