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 |
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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