[No authors listed]
Type I interferons (IFN-I) protect us from viral infections. Signal transducer and activator of transcription 2 is a key component of interferon-stimulated gene factor 3 (ISGF3), which drives gene expression in response to IFN-I. Using electron microscopy, we found that, in naive cells, lacking the activating tyrosine phosphorylation, forms a heterodimer with in an inactive, anti-parallel conformation. A novel phosphorylation of on T404 promotes IFN-I signaling by disrupting the dimer, facilitating the tyrosine phosphorylation of 1 and 2 and enhancing the DNA-binding ability of ISGF3. IKK-ε, activated by virus infection, phosphorylates T404 directly. Mice with a T-A mutation at the corresponding residue (T403) are highly susceptible to virus infections. We conclude that T404 phosphorylation drives a critical conformational switch that, by boosting the response to IFN-I in infected cells, enables a swift and efficient antiviral defense.
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