DHX58
Domain
The RLR CTR domain is capable of inhibiting dimerization and signaling of RIGI and also facilitates binding of dsRNA.
Function
Acts as a regulator of RIGI and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to RIGI and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on RIG-I signaling may involve the following mechanisms: competition with RIGI for binding to the viral RNA, binding to RIGI and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by RIGI and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses and coronavirus SARS-CoV-2, and also to the bacterial pathogen Listeria monocytogenes (PubMed:31256877). Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.
Sequence Similarities
Belongs to the helicase family. RLR subfamily.
Tissue Specificity
Expressed in testis, nerve and spleen. Also expressed in the brain.
Cellular localization
- Cytoplasm
Alternative names
D11LGP2E, LGP2, DHX58, ATP-dependent RNA helicase DHX58, ATP-dependent helicase LGP2, Protein D11Lgp2 homolog, RIG-I-like receptor 3, RIG-I-like receptor LGP2, RLR-3, RLR