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The TBK1-binding domain of optineurin promotes type I interferon responses (CROSBI ID 243646)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Meena, Netra Pal ; Zhu, Guozhi ; Mittelstadt, Paul R. ; Giardino Torchia, Maria Letizia ; Pourcelot, Marie ; Arnoult, Damien ; Ashwell, Jonathan D. ; Munitić, Ivana The TBK1-binding domain of optineurin promotes type I interferon responses // FEBS letters, 590 (2016), 10; 1498-1508. doi: 10.1002/1873-3468.12176

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

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Podaci o izdanju

590 (10)

2016.

1498-1508

objavljeno

0014-5793

1873-3468

10.1002/1873-3468.12176

Povezanost rada

Biologija

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