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• W2136824768 abstract "Abstract Recognition of RNA virus through TLR and RIG-I–like receptor results in rapid expression of type I IFNs, which play an essential role in host antiviral responses. However, the mechanisms to terminate the production of type I IFNs are not well defined. In the current study, we identified a member of the tripartite motif (TRIM) family, TRIM38, as a negative regulator in TLR3/4- and RIG-I–mediated IFN-β signaling. Knockdown of TRIM38 expression by small interfering RNA resulted in augmented activation of IFN regulatory factor 3 and enhanced expression of IFN-β, whereas overexpression of TRIM38 had opposite effects. Coimmunoprecipitation and colocalization experiments demonstrated that TRIM38 interacted with NF-κB–activating kinase-associated protein 1 (NAP1), which is required for TLR-induced IFN regulatory factor 3 activation and IFN-β production. As an E3 ligase, TRIM38 promoted K48-linked polyubiquitination and proteasomal degradation of NAP1. Thus, knockdown of TRIM38 expression resulted in higher protein level of NAP1 in primary macrophages. Consistent with the inhibitory roles in TLR3/4- and RIG-I–mediated IFN-β signaling, knockdown of TRIM38 significantly inhibited the replication of vesicular stomatitis virus. Overexpression of TRIM38 resulted in enhanced replication of vesicular stomatitis virus. Therefore, our results demonstrate that TRIM38 is a negative regulator for TLR and RIG-I–mediated IFN-β production by targeting NAP1 for ubiquitination and subsequent proteasome-mediated degradation." @default.
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• W2136824768 date "2012-06-01" @default.
• W2136824768 modified "2023-10-01" @default.
• W2136824768 title "Tripartite Motif-Containing Protein 38 Negatively Regulates TLR3/4- and RIG-I–Mediated IFN-β Production and Antiviral Response by Targeting NAP1" @default.
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• W2136824768 doi "https://doi.org/10.4049/jimmunol.1103506" @default.
• W2136824768 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22539786" @default.
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