Abstract:
: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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Cotton TR,Lechtenberg BCdoi
10.1042/BST20200237subject
Has Abstractpub_date
2020-08-28 00:00:00pages
1737-1750issue
4eissn
0300-5127issn
1470-8752pii
225819journal_volume
48pub_type
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