Non-lysine ubiquitylation: Doing things differently

Ian R. Kelsall (Lead / Corresponding author)

Research output: Contribution to journalReview articlepeer-review

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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 languageEnglish
Article number1008175
Number of pages28
JournalFrontiers in molecular biosciences
Volume9
DOIs
Publication statusPublished - 19 Sep 2022

Keywords

  • ubiquitin
  • oxyester bond
  • thioester bond
  • non-lysine ubiquitylation
  • ERAD
  • LUBAC
  • non-canonical ubiquitylation
  • RNF213
  • Rnf213

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