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- W4375954798 abstract "Type I interferons are important antiviral cytokines, but prolonged interferon production is detrimental to the host. The TLR3-driven immune response is crucial for mammalian antiviral immunity, and its intracellular localization determines induction of type I interferons; however, the mechanism terminating TLR3 signaling remains obscure. Here, we show that the E3 ubiquitin ligase ZNRF1 controls TLR3 sorting into multivesicular bodies/lysosomes to terminate signaling and type I interferon production. Mechanistically, c-Src kinase activated by TLR3 engagement phosphorylates ZNRF1 at tyrosine 103, which mediates K63-linked ubiquitination of TLR3 at lysine 813 and promotes TLR3 lysosomal trafficking and degradation. ZNRF1-deficient mice and cells are resistant to infection by encephalomyocarditis virus and SARS-CoV-2 because of enhanced type I interferon production. However, Znrf1-/- mice have exacerbated lung barrier damage triggered by antiviral immunity, leading to enhanced susceptibility to respiratory bacterial superinfections. Our study highlights the c-Src-ZNRF1 axis as a negative feedback mechanism controlling TLR3 trafficking and the termination of TLR3 signaling." @default.
- W4375954798 created "2023-05-10" @default.
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- W4375954798 date "2023-05-09" @default.
- W4375954798 modified "2023-10-14" @default.
- W4375954798 title "The Src–ZNRF1 axis controls TLR3 trafficking and interferon responses to limit lung barrier damage" @default.
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- W4375954798 doi "https://doi.org/10.1084/jem.20220727" @default.
- W4375954798 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37158982" @default.
- W4375954798 hasPublicationYear "2023" @default.
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