RIG-I

DEAD (Asp-Glu-Ala-Asp) box polypeptide 58

Rendering based on PDB 2QFB.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsDDX58 ; RIG-I; RIGI; RLR-1
External IDsOMIM: 609631 MGI: 2442858 HomoloGene: 32215 GeneCards: DDX58 Gene
EC number3.6.4.13
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez23586230073
EnsemblENSG00000107201ENSMUSG00000040296
UniProtO95786Q6Q899
RefSeq (mRNA)NM_014314NM_172689
RefSeq (protein)NP_055129NP_766277
Location (UCSC)Chr 9:
32.46 – 32.53 Mb		Chr 4:
40.2 – 40.24 Mb
PubMed search

RIG-I (retinoic acid-inducible gene 1) is a RIG-I-like receptor dsRNA helicase enzyme that is encoded (in humans) by the DDX58 gene. RIG-I is part of the RIG-I-like receptor family, which also includes MDA5 and LGP2, and functions as a pattern recognition receptor that is a sensor for viruses such as influenza A, Sendai virus, and flavivirus, however RIG-I provides no immunity to DNA viruses or retroviruses. RIG-I typically recognizes short (< 4000nt) 5′ triphosphate uncapped double stranded or single stranded RNA.[1][2][3] RIG-I and MDA5 are involved in activating MAVS and triggering an antiviral response.[4] RIG-I is also able to detect non-self 5′-triphosphorylated dsRNA transcribed from AT-rich dsDNA by DNA-dependent RNA polymerase III (Pol III). For many viruses, effective RIG-I-mediated antiviral responses are dependent on functionally active LGP2.[5]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases which are implicated in a number of cellular processes involving RNA binding and alteration of RNA secondary structure. RIG-I contains a RNA helicase-DEAD box motifs and a caspase recruitment domain (CARD). RIG-I is involved in viral double-stranded (ds) RNA recognition and the regulation of immune response.[6]

References

  1. ↑ Pichlmair, A. (2006). "RIG-I-Mediated Antiviral Responses to Single-Stranded RNA Bearing 5'-Phosphates". Science 314 (5801): 997–1001. doi:10.1126/science.1132998.
  2. ↑ Yoneyama M, Kikuchi M, Natsukawa T et al. (July 2004). "The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses". Nature Immunology 5 (7): 730–7. doi:10.1038/ni1087. PMID 15208624.
  3. ↑ Kato H, Takeuchi O, Mikamo-Satoh E, Hirai R, Kawai T, Matsushita K, Hiiragi A, Dermody TS, Fujita T, Akira S. (Jul 2008). "Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5.". J Exp Med. 205 (7): 1601–1610. doi:10.1084/jem.20080091. PMC 2442638. PMID 18591409.
  4. ↑ Hou, F; Sun, L; Zheng, H; Skaug, B; Jiang, QX; Chen, ZJ (Aug 5, 2011). "MAVS forms functional prion-like aggregates to activate and propagate antiviral innate immune response.". Cell 146 (3): 448–61. doi:10.1016/j.cell.2011.06.041. PMC 3179916. PMID 21782231.
  5. ↑ Satoh T, Kato H, Kumagai Y, Yoneyama M, Sato S, Matsushita K, Tsujimura T, Fujita T, Akira S, Takeuchi O (January 2010). "LGP2 is a positive regulator of RIG-I- and MDA5-mediated antiviral responses". Proc. Natl. Acad. Sci. U.S.A. 107 (4): 1512–7. doi:10.1073/pnas.0912986107. PMC 2824407. PMID 20080593.
  6. ↑ "Entrez Gene: DDX58 DEAD (Asp-Glu-Ala-Asp) box polypeptide 58".


Further reading