Ester-linked ubiquitination by HOIL-1 controls immune signalling by shaping the linear ubiquitin landscape

Jonathan N. Pruneda*, Rune Busk Damgaard*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Ester-linked ubiquitination of serine or threonine residues - or even lipids - has emerged as a new regulatory earmark in cell signalling. Petrova et al. (2021) now reveal that ubiquitin esterification by the atypical ubiquitin ligase HOIL-1, a component of the LUBAC complex, is critical for proper formation of linear ubiquitin chains and control of immune signalling in T cells and macrophages. Surprisingly, ester-linked ubiquitination can either promote or inhibit linear ubiquitin conjugation and cytokine production depending on the receptor and immune cell engaged. Comment on: https://doi.org/10.1111/febs.15896.
Original languageEnglish
JournalFEBS Journal
Number of pages6
ISSN1742-464X
DOIs
Publication statusAccepted/In press - 2021

Keywords

  • HOIL-1
  • Immune signalling
  • Inflammation
  • LUBAC
  • Ubiquitin

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