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http://purl.uniprot.org/citations/17392790http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17392790http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17392790http://www.w3.org/2000/01/rdf-schema#comment"Retinoic-acid-inducible gene-I (RIG-I; also called DDX58) is a cytosolic viral RNA receptor that interacts with MAVS (also called VISA, IPS-1 or Cardif) to induce type I interferon-mediated host protective innate immunity against viral infection. Furthermore, members of the tripartite motif (TRIM) protein family, which contain a cluster of a RING-finger domain, a B box/coiled-coil domain and a SPRY domain, are involved in various cellular processes, including cell proliferation and antiviral activity. Here we report that the amino-terminal caspase recruitment domains (CARDs) of RIG-I undergo robust ubiquitination induced by TRIM25 in mammalian cells. The carboxy-terminal SPRY domain of TRIM25 interacts with the N-terminal CARDs of RIG-I; this interaction effectively delivers the Lys 63-linked ubiquitin moiety to the N-terminal CARDs of RIG-I, resulting in a marked increase in RIG-I downstream signalling activity. The Lys 172 residue of RIG-I is critical for efficient TRIM25-mediated ubiquitination and for MAVS binding, as well as the ability of RIG-I to induce antiviral signal transduction. Furthermore, gene targeting demonstrates that TRIM25 is essential not only for RIG-I ubiquitination but also for RIG-I-mediated interferon-production and antiviral activity in response to RNA virus infection. Thus, we demonstrate that TRIM25 E3 ubiquitin ligase induces the Lys 63-linked ubiquitination of RIG-I, which is crucial for the cytosolic RIG-I signalling pathway to elicit host antiviral innate immunity."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.org/dc/terms/identifier"doi:10.1038/nature05732"xsd:string
http://purl.uniprot.org/citations/17392790http://purl.org/dc/terms/identifier"doi:10.1038/nature05732"xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Chen Z."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Liang C."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Liang C."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Inoue S."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Inoue S."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Jung J.U."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Jung J.U."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Sun L."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Sun L."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Akira S."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Akira S."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Urano T."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Urano T."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Joo C.H."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Joo C.H."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Shin Y.C."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Shin Y.C."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Takeuchi O."xsd:string
http://purl.uniprot.org/citations/17392790http://purl.uniprot.org/core/author"Takeuchi O."xsd:string