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.
Bibliographical noteFunding Information:
We thank K. Iwai for GST-hTNFα(77–233) cDNA, S. Yonehara for Flag-MST1 cDNA, V.M. Dixit for antibody to linear ubiquitin, S.Y. Lee for TRAF2 +/+ or TRAF2 − / − MEFs, and D.S. Lim for MST1 − / − mice. This work was supported by a National Research Foundation grant ( NRF-2017R1A2B2008193 ) and by a BRL grant ( NRF-2015R1A4A1041919 ) funded by the Ministry of Science and ICT of Korea as well as by a Korea University grant (E.-J.C.).
© 2019 Elsevier Inc.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology