Panne, DanielMcWhirter, Sarah M.Maniatis, TomHarrison, Stephen C.2019-10-132007Panne, Daniel, Sarah M. McWhirter, Tom Maniatis, and Stephen C. Harrison. 2007. “Interferon Regulatory Factor 3 Is Regulated by a Dual Phosphorylation-Dependent Switch.” Journal of Biological Chemistry 282 (31): 22816–22. doi:10.1074/jbc.M703019200.0021-92581083-351Xhttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41542802The transcription factor interferon regulatory factor 3 (IRF-3) regulates genes in the innate immune response. IRF-3 is activated through phosphorylation by the kinases IKK is an element of and/or TBK1. Phosphorylation results in IRF-3 dimerization and removal of an autoinhibitory structure to allow interaction with the coactivators CBP/p300. The precise role of the different phosphorylation sites has remained controversial. Using purified proteins we show that TBK1 can directly phosphorylate full-length IRF-3 in vitro. Phosphorylation at residues in site 2 (Ser(396) - Ser(405)) alleviates autoinhibition to allow interaction with CBP (en-USJournal Article2019-10-1310.1074/jbc.M703019200