RACK1 T50 Phosphorylation by AMPK Potentiates Its Binding with IRF3/7 and Inhibition of Type 1 IFN Production

Abstract The receptor for activated C kinase 1 (RACK1) adaptor protein has been implicated in viral infection. However, whether RACK1 promotes vivo infection mammals remains unknown. Moreover, it elusive how is engaged antiviral innate immune signaling. In this study, we report that myeloid deficiency does not affect the development and survival of cells under resting conditions but renders mice less susceptible to RACK1-deficient macrophages produce more IFN-? IFN-? response both RNA DNA virus line with this, suppresses transcriptional activation type IFN gene promoters Analysis virus-mediated signaling indicates inhibits phosphorylation IRF3/7. Indeed, interacts IRF3/7, which enhanced after Further exploration triggers AMPK activation, turn phosphorylates at Thr50. Thr50 enhances its interaction IRF3/7 thereby limits phosphorylation. Thus, our results confirm provide insight into control production