viral dsRNA binds IFIH1:DAK

Stable Identifier
R-HSA-913725
Type
Reaction
Species
Homo sapiens
Related Species
Measles virus, Influenza A virus
Compartment
Synonyms
dsRNA binds to MDA5
Locations in the PathwayBrowser
Summation

Interferon-induced helicase C domain-containing protein 1 (IFIH1, MDA5) is the closest relative of Probable ATP-dependent RNA helicase DDX58 (DDX58, RIG-I). It contains two Caspase activation and recruitment domain (CARD)-like regions, a DExD/H helicase domain, and a C-terminal region similar to the RD of DDX58. IFIH1, via its C-terminal domain (CTD), preferentially binds dsRNA with blunt ends. It does not associate with dsRNA having 5' or 3' overhangs. Upon binding dsRNA, IFIH1 is presumed to undergo a structural alteration that unmasks the CARDs enabling them to recruit downstream signal transducer proteins. Dihydroxyacetone kinase (DAK) binds to the CARD domains of IFIH1, acting as a negative regulator. It is released upon the conformational change induced by viral RNA binding, allowing the CARD domains to bind to the CARD of Mitochondrial antiviral-signaling protein (MAVS, IPS-1).

Literature References
PubMed ID Title Journal Year
18591409 Length-dependent recognition of double-stranded ribonucleic acids by retinoic acid-inducible gene-I and melanoma differentiation-associated gene 5

Kato, H, Takeuchi, O, Mikamo-Satoh, E, Hirai, R, Kawai, T, Matsushita, K, Hiiragi, A, Dermody, TS, Fujita, T, Akira, S

J Exp Med 2008
19531363 Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5

Li, X, Lu, C, Stewart, M, Xu, H, Strong, RK, Igumenova, T, Li, P

Arch Biochem Biophys 2009
17600090 Negative regulation of MDA5- but not RIG-I-mediated innate antiviral signaling by the dihydroxyacetone kinase

Diao, F, Li, S, Tian, Y, Zhang, M, Xu, LG, Zhang, Y, Wang, RP, Chen, D, Zhai, Z, Zhong, B, Tien, P, Shu, HB

Proc Natl Acad Sci U S A 2007
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