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) |
|---|---|
| Pages (from-to) | 5903-5908 |
| Number of pages | 6 |
| Journal | FEBS Journal |
| Volume | 288 |
| Issue number | 20 |
| DOIs |
|
| State | Published - Oct 2021 |
Funding
The authors acknowledge funding and support from the Novo Nordisk Foundation and the Technical University of Denmark (to RBD) and Oregon Health & Science University (to JNP). The figures were created using https://biorender.com .
| Funders |
|---|
| Oregon State University/Oregon Health and Science University |
| Danmarks Tekniske Universitet |
| Novo Nordisk Fonden |
Keywords
- HOIL-1
- LUBAC
- immune signalling
- inflammation
- ubiquitin
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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