| First Author | Liu H | Year | 2021 |
| Journal | iScience | Volume | 24 |
| Issue | 2 | Pages | 102078 |
| PubMed ID | 33644712 | Mgi Jnum | J:343880 |
| Mgi Id | MGI:6717874 | Doi | 10.1016/j.isci.2021.102078 |
| Citation | Liu H, et al. (2021) The tyrosine kinase c-Abl potentiates interferon-mediated antiviral immunity by STAT1 phosphorylation. iScience 24(2):102078 |
| abstractText | Interferon (IFN)-induced activation of the signal transducer and activator of transcription (STAT) family is an important event in antiviral immunity. Here, we show that the nonreceptor kinases c-Abl and Arg directly interact with STAT1 and potentiate the phosphorylation of STAT1 on Y701. c-Abl/Arg could mediate STAT1 phosphorylation independent of Janus kinases in the absence of IFNgamma and potentiate IFNgamma-mediated STAT1 phosphorylation. Moreover, STAT1 dimerization, nuclear translocation, and downstream gene transcription are regulated by c-Abl/Arg. c-Abl/Arg (abl1/abl2) deficiency significantly suppresses antiviral responses in vesicular stomatitis virus-infected cells. Compared to vehicle, administration of the c-Abl/Arg selective inhibitor AMN107 resulted in significantly increased mortality in mice infected with human influenza virus. Our study demonstrates that c-Abl plays an essential role in the STAT1 activation signaling pathway and provides an important approach for antiviral immunity regulation. |
