c-Abl tyrosine kinase interacts with MAVS and regulates innate immune response

The tyrosine kinase, c-Abl, plays important roles in many aspects of cellular function. Previous reports showed that c-Abl is involved in NF-κB signaling. However, the functions of c-Abl in innate immunity are still unknown. Here we demonstrate that the mitochondrial antiviral signaling (MAVS) protein can be physically associated with c-Abl in vivo and in vitro. MAVS interacted with c-Abl through its Card and TM domain. A phosphotyrosine-specific antibody indicated that MAVS was phosphorylated by c-Abl. Functional impairment of c-Abl attenuated MAVS or VSV induced type-I IFN production. Importantly, c-Abl knockdown in MCF7 cells displayed impaired MAVS-mediated NF-κB and IRF3 activation. Taken together, our results suggest that c-Abl modulates innate immune response through MAVS. MINT- 7297498, MINT- 7297511, MINT- 7297557, MINT- 7297574: MAVS (uniprotkb: Q7Z434) physically interacts (MI: 0915) with c-Abl (uniprotkb: P00519) by anti tag coimmunoprecipitation (MI: 0007)MINT- 7297542: c-Abl (uniprotkb: P00519) physically interacts (MI: 0915) with MAVS (uniprotkb: Q7Z434) by anti bait coimmunoprecipitation (MI: 0006)MINT- 7297526: c-Abl (uniprotkb: P00519) physically interacts (MI: 0915) with MAVS (uniprotkb: Q7Z434) by far western blotting (MI: 0047)