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The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling.

Antiviral immune responses are initiated through Toll-like receptors (TLRs) and RIG-I (retinoic acid-inducible gene-I)-like RNA helicases that recognize nucleic acids from distinct viruses. In this study, we show that the tyrosine kinase c-Src participates in antiviral responses induced by the cytoplasmic RNA helicase RIG-I. Sendai virus (SV), which is recognized by RIG-I, induced c-Src phosphorylation. Functional impairment of c-Src through chemical inhibition or transient expression of a c-Src kinase-inactive mutant attenuated production of endogenous antiviral proteins after SV infection or after expression of RIG-I or its adapter protein MAVS. Importantly, SV-stimulated synthesis of antiviral proteins was significantly impaired in cells treated with c-Src small interfering RNA and in cells from c-Src-deficient mice. In addition, we found that c-Src interacted with components of the RIG-I pathway: RIG-I, MAVS, and TRAF3 (tumor necrosis factor receptor-associated factor-3). The interaction between c-Src and TRAF3 was found to occur within the RING domain of TRAF3. Taken together, our results suggest that c-Src enhances RIG-I-mediated signaling, acting at the level of TRAF3.

Pubmed ID: 19419966 RIS Download

Mesh terms: Animals | Antiviral Agents | DEAD Box Protein 58 | DEAD-box RNA Helicases | Gene Expression Regulation | Genes, Reporter | Humans | Interferon Regulatory Factor-3 | Mice | Models, Biological | RNA, Small Interfering | Sendai virus | Signal Transduction | TNF Receptor-Associated Factor 3 | src-Family Kinases

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Associated grants

  • Agency: NIAID NIH HHS, Id: R01 AI067497
  • Agency: NIAID NIH HHS, Id: R01 AI067497-01
  • Agency: NIAID NIH HHS, Id: R01 AI067497-05

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