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• W2904017346 abstract "Abstract Retinoic acid inducible gene-I (RIG-I) ensures immune surveillance of viral RNAs bearing a 5’-triphosphate (5’ppp) moiety. Mutations in RIG-I (C268F and E373A) lead to impaired ATPase activity, thereby driving hyperactive signaling associated with autoimmune diseases. Here we report, using hydrogen/deuterium exchange, mechanistic models for dysregulated RIG-I proofreading that ultimately result in the improper recognition of cellular RNAs bearing 7-methylguanosine and N 1 -2’-O-methylation (Cap1) on the 5’ end. Cap1-RNA compromises its ability to stabilize RIG-I helicase and blunts caspase activation and recruitment domains (CARD) partial opening by threefold. RIG-I H830A mutation restores Cap1-helicase engagement as well as CARDs partial opening event to a level comparable to that of 5’ppp. However, E373A RIG-I locks the receptor in an ATP-bound state, resulting in enhanced Cap1-helicase engagement and a sequential CARDs stimulation. C268F mutation renders a more tethered ring architecture and results in constitutive CARDs signaling in an ATP-independent manner." @default.
• W2904017346 created "2018-12-22" @default.
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• W2904017346 date "2018-12-18" @default.
• W2904017346 modified "2023-10-11" @default.
• W2904017346 title "HDX-MS reveals dysregulated checkpoints that compromise discrimination against self RNA during RIG-I mediated autoimmunity" @default.
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• W2904017346 doi "https://doi.org/10.1038/s41467-018-07780-z" @default.
• W2904017346 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6299088" @default.
• W2904017346 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30560918" @default.
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