| First Author | Song Y | Year | 2017 |
| Journal | Nat Commun | Volume | 8 |
| Pages | 14654 | PubMed ID | 28287082 |
| Mgi Jnum | J:244688 | Mgi Id | MGI:5913467 |
| Doi | 10.1038/ncomms14654 | Citation | Song Y, et al. (2017) E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses. Nat Commun 8:14654 |
| abstractText | Viruses can escape from host recognition by degradation of RIG-I or interference with the RIG-I signalling to establish persistent infections. However, the mechanisms by which host cells stabilize RIG-I protein for avoiding its degradation are largely unknown. We report here that, upon virus infection, the E3 ubiquitin ligase FBXW7 translocates from the nucleus into the cytoplasm and stabilizes RIG-I. FBXW7 interacts with SHP2 and mediates the degradation and ubiquitination of SHP2, thus disrupting the SHP2/c-Cbl complex, which mediates RIG-I degradation. When infected with VSV or influenza A virus, FBXW7 conditional knockout mice (Lysm+FBXW7f/f) show impaired antiviral immunity. FBXW7-deficient macrophages have decreased RIG-I protein levels and type-I interferon signalling. Furthermore, PBMCs from RSV-infected children have reduced FBXW7 mRNA levels. Our results identify FBXW7 as an important interacting partner for RIG-I. These findings provide insights into the function of FBXW7 in antiviral immunity and its related clinical significance. |
