ArticleNucleic acids research2017
Selective RNA targeting and regulated signaling by RIG-I is controlled by coordination of RNA and ATP binding.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- A two-step mechanism for RIG-I activation by influenza virus mvRNAs.Science advances · 2025Article
- The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.Molecular cell · 2022Article
- The molecular mechanism of RIG-I activation and signaling.Immunological reviews · 2021Review
- Insights into the structure and RNA-binding specificity of Caenorhabditis elegans Dicer-related helicase 3 (DRH-3).Nucleic acids research · 2021Article
- Innate Inhibiting Proteins Enhance Expression and Immunogenicity of Self-Amplifying RNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2021Article
- DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.Nucleic acids research · 2020Article
- Establishment of a Replicon Reporter of the Emerging Tick-Borne Bourbon Virus and Use It for Evaluation of Antivirals.Frontiers in microbiology · 2020Article
- RNA binding activates RIG-I by releasing an autorepressed signaling domain.Science advances · 2019Article
- DHX15 Is a Coreceptor for RLR Signaling That Promotes Antiviral Defense Against RNA Virus Infection.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2019Article
- Significance and Role of Pattern Recognition Receptors in Malignancy.Archivum immunologiae et therapiae experimentalis · 2019Review
- Discrimination of cytosolic self and non-self RNA by RIG-I-like receptors.The Journal of biological chemistry · 2017Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
RIG-I is an innate immune receptor that detects and responds to infection by deadly RNA viruses such as influenza, and Hepatitis C. In the cytoplasm, RIG-I is faced with a difficult challenge: it must sensitively detect viral RNA while ignoring the abundance of host RNA. It has been suggested that RIG-I has a ‘proof-reading’ mechanism for rejecting host RNA targets, and that disruptions of this selectivity filter give rise to autoimmune diseases. Here, we directly monitor RNA proof-reading by RIG-I and we show that it is controlled by a set of conserved amino acids that couple RNA and ATP binding to the protein (Motif III). Mutations of this motif directly modulate proof-reading by eliminating or enhancing selectivity for viral RNA, with major implications for autoimmune disease and cancer. More broadly, the results provide a physical explanation for the ATP-gated behavior of SF2 RNA helicases and receptor proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.