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Abstract
The post-translational modification of proteins with ubiquitin plays a central role in nearly all aspects of eukaryotic biology. Historically, studies have focused on the conjugation of ubiquitin to lysine residues in substrates, but it is now clear that ubiquitylation can also occur on cysteine, serine, and threonine residues, as well as on the N-terminal amino group of proteins. Paradigm-shifting reports of non-proteinaceous substrates have further extended the reach of ubiquitylation beyond the proteome to include intracellular lipids and sugars. Additionally, results from bacteria have revealed novel ways to ubiquitylate (and deubiquitylate) substrates without the need for any of the enzymatic components of the canonical ubiquitylation cascade. Focusing mainly upon recent findings, this review aims to outline the current understanding of non-lysine ubiquitylation and speculate upon the molecular mechanisms and physiological importance of this non-canonical modification.
Original language | English |
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Article number | 1008175 |
Number of pages | 28 |
Journal | Frontiers in Molecular Biosciences |
Volume | 9 |
DOIs | |
Publication status | Published - 19 Sept 2022 |
Keywords
- ubiquitin
- oxyester bond
- thioester bond
- non-lysine ubiquitylation
- ERAD
- LUBAC
- non-canonical ubiquitylation
- RNF213
- Rnf213
ASJC Scopus subject areas
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology (miscellaneous)
- Biochemistry
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Dive into the research topics of 'Non-lysine ubiquitylation: Doing things differently'. Together they form a unique fingerprint.Projects
- 1 Finished
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The Molecular Mechanisms by which TRAF6 Regulates the Immune System
Cohen, P. (Investigator)
1/04/18 → 31/03/24
Project: Research