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 language | English (US) |
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Pages (from-to) | 5903-5908 |
Number of pages | 6 |
Journal | FEBS Journal |
Volume | 288 |
Issue number | 20 |
DOIs |
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State | Published - Oct 2021 |
Keywords
- HOIL-1
- LUBAC
- immune signalling
- inflammation
- ubiquitin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology