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• W2289655038 endingPage "628" @default.
• W2289655038 startingPage "613" @default.
• W2289655038 abstract "Type I interferon (IFN) is an important component of antiviral innate immune signaling mediated by viral DNA and RNA recognition by the DNA sensor cGAS and RNA sensors RIG-I and MDA5. Activation of these DNA and RNA sensors leads to the recruitment of STING and MAVS, respectively, and converges on TANK-binding kinase 1 (TBK1) signaling for subsequent phosphorylation of IFN regulatory factor 3 (IRF3). However, the mechanisms that control TBK1 activation are still poorly defined. Here, we identify tripartite motif 9 short isoform (TRIM9s) as a positive regulator in type I IFN signaling. Upon viral infection, TRIM9s undergoes Lys-63-linked auto-polyubiquitination and serves as a platform to bridge GSK3β to TBK1, leading to the activation of IRF3 signaling. Interestingly, we found that TRIM9s selectively inhibits the production of pro-inflammatory cytokines, but enhances the expression of type I IFNs as well as IFN-stimulated genes, in response to viral infection. Our findings reveal novel dual functions of TRIM9s in antiviral immunity, which serve to balance pro-inflammatory response and production of type I IFNs." @default.
• W2289655038 created "2016-06-24" @default.
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• W2289655038 date "2016-02-26" @default.
• W2289655038 modified "2023-10-13" @default.
• W2289655038 title "TRIM9 short isoform preferentially promotes DNA and RNA virus-induced production of type I interferon by recruiting GSK3β to TBK1" @default.
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• W2289655038 doi "https://doi.org/10.1038/cr.2016.27" @default.
• W2289655038 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4856760" @default.
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• W2289655038 hasPublicationYear "2016" @default.
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