| First Author | Zhou Y | Year | 2016 |
| Journal | Nat Immunol | Volume | 17 |
| Issue | 4 | Pages | 397-405 |
| PubMed ID | 26928339 | Mgi Jnum | J:259954 |
| Mgi Id | MGI:6141752 | Doi | 10.1038/ni.3395 |
| Citation | Zhou Y, et al. (2016) The kinase CK1varepsilon controls the antiviral immune response by phosphorylating the signaling adaptor TRAF3. Nat Immunol 17(4):397-405 |
| abstractText | The signaling adaptor TRAF3 is a highly versatile regulator of both innate immunity and adaptive immunity, but how its phosphorylation is regulated is still unknown. Here we report that deficiency in or inhibition of the conserved serine-threonine kinase CK1varepsilon suppressed the production of type I interferon in response to viral infection. CK1varepsilon interacted with and phosphorylated TRAF3 at Ser349, which thereby promoted the Lys63 (K63)-linked ubiquitination of TRAF3 and subsequent recruitment of the kinase TBK1 to TRAF3. Consequently, CK1varepsilon-deficient mice were more susceptible to viral infection. Our findings establish CK1varepsilon as a regulator of antiviral innate immune responses and indicate a novel mechanism of immunoregulation that involves CK1varepsilon-mediated phosphorylation of TRAF3. |
