p-PKR dimer phosphorylates ILF3:ILF2

Stable Identifier
Reaction [transition]
Homo sapiens
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Activated PKR phosphorylates interleukin enhancer-binding factor 3 (also known as NF90, NFAR, DRBP76, MBP4, or ILF3) at residues T188 and T315, resulting in dissociation of p-ILF3 from its complex with ILF2, retaining and accumulating p-ILF3 in the cytosol. On viral infection, cytosolic p-ILF3 binds to viral mRNA, inhibiting its translation. Since ILF3 also activates PKR, both processes appear to be part of a feedback loop, enhancing PKR signaling (Ting et al, 1998; Patel et al, 1999; Harashima et al, 2010).
Literature References
PubMed ID Title Journal Year
10400669 DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR

Patel, RC, Guo, W, Williams, BR, Xu, Z, Sen, GC, Bandyopadhyay, S, Vestal, DJ, Erme, SM

J Biol Chem 1999
21123651 Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense

Harashima, A, Guettouche, T, Barber, GN

Genes Dev 2010
9442054 DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45

Lees-Miller, SP, Kao, PN, Lintott, LG, Ting, NS, Chan, DW

J Biol Chem 1998
Catalyst Activity

protein kinase activity of p-EIF2AK2 dimer [cytosol]

Orthologous Events
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