Identification of a novel in vivo virus-targeted phosphorylation site in interferon regulatory factor-3 (IRF3).

ABSTRACT: The transcription factor interferon regulatory factor-3 (IRF3) regulates expression of type I interferon-beta and plays an important role in antiviral immunity. Despite the biological importance of IRF3, its in vivo phosphorylation pattern has not been reported. In this study, we have identified residues in IRF3 that are phosphorylated in vivo after infection with Sendai virus. We found that Sendai virus induced phosphorylation of the C-terminal residues Thr(390) and Ser(396), in addition to either Ser(385) or Ser(386). Moreover, Ser(173) and Ser(175) were constitutively phosphorylated. Ser(396) has previously been suggested to be the major target of the IRF3-activating kinase TBK1 (TANK-binding kinase-1), whereas Thr(390) has not previously been implicated in IRF3 regulation. Mutagenesis

SUBMITTER: Bergstroem B 

PROVIDER: S-EPMC2915726 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature