DHX36 enhances RIG-I signaling by facilitating PKR-mediated antiviral stress granule formation.

DOI IR (HANDLE) HANDLE Web Site PubMed 14 Citations 43 References Open Access

Description

RIG-I is a DExD/H-box RNA helicase and functions as a critical cytoplasmic sensor for RNA viruses to initiate antiviral interferon (IFN) responses. Here we demonstrate that another DExD/H-box RNA helicase DHX36 is a key molecule for RIG-I signaling by regulating double-stranded RNA (dsRNA)-dependent protein kinase (PKR) activation, which has been shown to be essential for the formation of antiviral stress granule (avSG). We found that DHX36 and PKR form a complex in a dsRNA-dependent manner. By forming this complex, DHX36 facilitates dsRNA binding and phosphorylation of PKR through its ATPase/helicase activity. Using DHX36 KO-inducible MEF cells, we demonstrated that DHX36 deficient cells showed defect in IFN production and higher susceptibility in RNA virus infection, indicating the physiological importance of this complex in host defense. In summary, we identify a novel function of DHX36 as a critical regulator of PKR-dependent avSG to facilitate viral RNA recognition by RIG-I-like receptor (RLR).

Journal

  • PLoS pathogens

    PLoS pathogens 10 (3), e1004012-, 2014-03-20

    Public Library of Science

Citations (14)*help

See more

References(43)*help

See more

Related Projects

See more

Keywords

Details 詳細情報について

Report a problem

Back to top