viral dsRNA binds DDX58

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Rotavirus, Influenza A virus, Hepatitis C Virus
dsRNA binds to RIG-I
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Probable ATP-dependent RNA helicase DDX58 (DDX58, RIG-I, RIG-1) has two caspase recruitment domains (CARD) in its N-terminus, a DExD/H helicase domain with an ATP binding motif in the middle and a repressor domain (RD) in the C-terminus. In the absence of appropriate stimulation, DDX58 is in a 'closed' conformation in which the repressor domain phyically interacts with the helicase domain masking CARD. Upon viral infection, the free triphosphate structure at the 5' end of viral RNAs activates DDX58 by binding to its RNA helicase domain. This provokes a change in DDX58 conformation exposing the CARD leading to DDX58 dimerization, allowing it to interact with 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
15208624 The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses

Yoneyama, M, Kikuchi, M, Natsukawa, T, Shinobu, N, Imaizumi, T, Miyagishi, M, Taira, K, Fujita, T

Nat Immunol 2004
Participant Of
This event is regulated
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