Abstract
Lee et al. identify MST1 as a component of TNF-RSC that phosphorylates HOIP at serine 1,066 and thereby inhibits the linear ubiquitin chain-forming activity of LUBAC in a TRAF2-dependent manner. MST1, by inhibiting an E3 ligase activity of HOIP, negatively regulates the NF-κB-dependent inflammatory gene expression induced by TNFα.
| Original language | English |
|---|---|
| Pages (from-to) | 1138-1149.e6 |
| Journal | Molecular Cell |
| Volume | 73 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2019 Mar 21 |
Bibliographical note
Publisher Copyright:© 2019 Elsevier Inc.
Keywords
- HOIP
- LUBAC
- MST1
- NF-κB
- TNFα
- TNFα receptor 1 signaling complex
- TRAF2
- inflammation
- macrophage
- ubiquitination
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Fingerprint
Dive into the research topics of 'MST1 Negatively Regulates TNFα-Induced NF-κB Signaling through Modulating LUBAC Activity'. Together they form a unique fingerprint.Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS