The TBK1-binding domain of optineurin promotes type I interferon responses (CROSBI ID 243646)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Meena, Netra Pal ; Zhu, Guozhi ; Mittelstadt, Paul R. ; Giardino Torchia, Maria Letizia ; Pourcelot, Marie ; Arnoult, Damien ; Ashwell, Jonathan D. ; Munitić, Ivana
engleski
The TBK1-binding domain of optineurin promotes type I interferon responses
Pathogen-associated molecular pattern (PAMP) recognition leads to TANK-binding kinase (TBK1) polyubiquitination and activation by transautophosphorylation, resulting in IFN-β production. Here, we describe a mouse model of optineurin insufficiency (OptnΔ157) in which the TBK1-interacting N-terminus of optineurin was deleted. PAMP-stimulated cells from OptnΔ157 mice had reduced TBK1 activity, no phosphorylation of optineurin Ser187, and mounted low IFN-β responses. In contrast to pull-down assays where the presence of N-terminus was sufficient for TBK1 binding, both the N-terminal and the ubiquitin-binding regions of optineurin were needed for PAMP-induced binding. This report establishes optineurin as a positive regulator TBK1 via a bipartite interaction between these molecules.
optineurin ; TBK1 ; type I interferon
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano