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

Jonathan N. Pruneda, Rune Busk Damgaard

Research output: Contribution to journalComment/debatepeer-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 (US)
Pages (from-to)5903-5908
Number of pages6
JournalFEBS Journal
Volume288
Issue number20
DOIs
StatePublished - Oct 2021

Keywords

  • HOIL-1
  • LUBAC
  • immune signalling
  • inflammation
  • ubiquitin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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