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http://purl.uniprot.org/citations/23843640http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23843640http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23843640http://www.w3.org/2000/01/rdf-schema#comment"Retinoic acid-inducible gene I (RIG-I) is a key sensor for recognizing nucleic acids derived from RNA viruses and triggers beta interferon (IFN-β) production. Because of its important role in antiviral innate immunity, the activity of RIG-I must be tightly controlled. Here, we used yeast two-hybrid screening to identify a SEC14 family member, SEC14L1, as a RIG-I-associated negative regulator. Transfected SEC14L1 interacted with RIG-I, and endogenous SEC14L1 associated with RIG-I in a viral infection-inducible manner. Overexpression of SEC14L1 inhibited transcriptional activity of the IFN-β promoter induced by RIG-I but not TANK-binding kinase 1 (TBK1) and interferon regulatory factor 3 (IRF3). Knockdown of endogenous SEC14L1 in both HEK293T cells and HT1080 cells potentiated RIG-I and Sendai virus-triggered IFN-β production as well as attenuated the replication of Newcastle disease virus. SEC14L1 interacted with the N-terminal domain of RIG-I (RIG-I caspase activation and recruitment domain [RIG-I-CARD]) and competed with VISA/MAVS/IPS-1/Cardif for RIG-I-CARD binding. Domain mapping further indicated that the PRELI-MSF1 and CRAL-TRIO domains but not the GOLD domain of SEC14L1 are required for interaction and inhibitory function. These findings suggest that SEC14L1 functions as a novel negative regulator of RIG-I-mediated antiviral signaling by preventing RIG-I interaction with the downstream effector."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.org/dc/terms/identifier"doi:10.1128/jvi.01073-13"xsd:string
http://purl.uniprot.org/citations/23843640http://purl.org/dc/terms/identifier"doi:10.1128/jvi.01073-13"xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Xu H."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Chen H.W."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Chen H.W."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Yang Y.K."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Yang Y.K."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Di W."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Di W."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Zhai Z.H."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Zhai Z.H."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Li M.T."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Li M.T."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Zhang F.X."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/author"Zhang F.X."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/23843640http://purl.uniprot.org/core/name"J. Virol."xsd:string