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• W2078830334 startingPage "546" @default.
• W2078830334 abstract "During viral infection, production of proinflammatory cytokines including type I interferons (IFNs) is under stringent control to avoid detrimental overreaction. The protein inhibitor of activated STAT (PIAS) family proteins have been recognized as anti-inflammatory molecules by restraining type I IFN induced amplifying signaling. Here we identified PIAS1 as an important negative regulator of virus-triggered type I IFN signaling. Overexpression of PIAS1 repressed virus-or RIG-I like receptor stimulated type I IFN transcription, whereas knockdown of PIAS1 expression augmented virus-induced production of type I IFNs. PIAS1 with a mutation in the SAP domain retained the inhibitory function in virus-induced IFN transcription, but abolished the inhibition in IFN-stimulated signaling. SUMO E3 ligase activity dead mutant PIAS1/C350S still had the comparable inhibitory function with WT PIAS1. Further study indicated that PIAS1 interacted with IRF3 and inhibited the DNA binding activity of IRF3. The C-terminal region of PIAS1 around a cluster of acidic amino acids is critical for the interaction with IRF3 and the inhibitory functions of PIAS1. Therefore, these results unveil PIAS1 functions both at the virus-induced early signaling stage and IFN stimulated amplifying stage with distinct mechanisms. PIAS1 is important in maintaining proper amounts of type I IFNs and restrains its magnitude when the antiviral response intensifies." @default.
• W2078830334 created "2016-06-24" @default.
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• W2078830334 date "2013-11-01" @default.
• W2078830334 modified "2023-10-17" @default.
• W2078830334 title "PIAS1 negatively modulates virus triggered type I IFN signaling by blocking the DNA binding activity of IRF3" @default.
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• W2078830334 doi "https://doi.org/10.1016/j.antiviral.2013.09.001" @default.
• W2078830334 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24036127" @default.
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