IRF3 is activated through a two-step phosphorylation in the C-terminal domain mediated by TBK1 and/or IKKi, requiring Ser386 and/or Ser385- site 1; and a cluster of serine/threonine residues between Ser396 and Ser405- site 2 [Panne et al 2007]. Phosphorylated residues at site 2 (Ser396 - Ser405) alleviate autoinhibition to allow interaction with CBP (CREB-binding protein) and facilitate phosphorylation at site 1 (Ser385 or Ser386). Phosphorylation at site 1 is required for IRF3 dimerization.
Panne, D, McWhirter, SM, Maniatis, T, Harrison, SC
Fitzgerald, KA, McWhirter, SM, Faia, KL, Rowe, DC, Latz, E, Golenbock, DT, Coyle, AJ, Liao, SM, Maniatis, T
Yoneyama, M, Suhara, W, Fukuhara, Y, Fukuda, M, Nishida, E, Fujita, T
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