Interferon Regulatory Factor 3 Is Regulated by a Dual Phosphorylation-dependent Switch
McWhirter, Sarah M.
Harrison, Stephen C.
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CitationPanne, 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.
AbstractThe 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 (
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