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 |
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Journal | FEBS Journal |
Volume | 288 |
Issue number | 20 |
Pages (from-to) | 5903-5908 |
Number of pages | 6 |
ISSN | 1742-464X |
DOIs | |
Publication status | Published - 2021 |
Keywords
- HOIL-1
- Immune signalling
- Inflammation
- LUBAC
- Ubiquitin