Serine/threonine-protein kinase TBK1 is a ~83 kDa protein. Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents. Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB. In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli. Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1. 1. Pomerantz, JL. et al. (1999) The EMBO journal 18, 6694-704. PMID: 105812432. Kishore, N. et al. (2002) The Journal of biological chemistry 277, 13840-7. PMID: 118397433. Fitzgerald, KA. et al. (2003) Nature immunology 4, 491-6. PMID: 126925494. Sharma, S. et al. (2003) Science (New York, N.Y.) 300, 1148-51. PMID: 127028065. Mori, M. et al. (2004) The Journal of biological chemistry 279, 9698-702. PMID: 147035136. tenOever, BR. et al. (2004) Journal of virology 78, 10636-49. PMID: 153676317. Kuai, J. et al. (2004) The Journal of biological chemistry 279, 53266-71. PMID: 154858378. Soulat, D. et al. (2008) The EMBO journal 27, 2135-46. PMID: 185839609. Clark, K. et al. (2011) The Biochemical journal 434, 93-104. PMID: 21138416 | 
