Research ArticleImmunology

The tyrosine kinase Src promotes phosphorylation of the kinase TBK1 to facilitate type I interferon production after viral infection

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Sci. Signal.  03 Jan 2017:
Vol. 10, Issue 460, eaae0435
DOI: 10.1126/scisignal.aae0435

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Src and interferon

Cells are armed with multiple pattern recognition receptors (PRRs) that sense viral infection. Although PRRs mediate signaling through different adaptor proteins, they mostly converge on activation of the kinase TBK1, which phosphorylates and activates the transcription factor IRF3 to promote expression of genes encoding type I interferons (IFNs). Li et al. found that TBK1, which undergoes serine autophosphorylation to become activated, was also tyrosine-phosphorylated, which was dependent on the kinase Src. Although Src did not directly associate with and phosphorylate TBK1, it was recruited to multiple PRR-associated adaptor-containing complexes that contained TBK1. Furthermore, loss of Src or inhibition of its activity impaired the production of type I IFNs by virally infected macrophages, suggesting that Src acts as a central regulator of the innate immune response to viruses.