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Updated: Sep 17, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
DYRK kinases phosphorylate IL-17RA at S801
Sayed Ala Moududee1, Andrew A Herppich2, Mary Kay H Pflum2
1Department of Structural & Cellular Biology, Tulane University School of Medicine, New Orleans, LA 70112, USA.
Abstract:
Interleukin-17 (IL-17) receptor A (IL-17RA) promotes inflammatory reactions by activating kinases and transcription regulators. Our previous studies have demonstrated that glycogen synthase kinase 3 (GSK3) phosphorylates IL-17RA at T780. It is not known whether other kinases also phosphorylate IL-17RA. Here, we identified an association between dual-specificity tyrosine-regulated kinases (DYRKs) and IL-17RA. We found that DYRK1B and DYRK4 interacted with and phosphorylated IL-17RA at serine 801 (S801). Overexpression of DYRK1B and DYRK4 enhanced IL-17RA phosphorylation, whereas siRNA-mediated knockdown of DYRK1B or DYRK4 reduced the phosphorylation. Serum starvation of the cultured cells increased expression levels of DYRK1B/4 and IL-17RA phosphorylation, suggesting stress-dependent modulation of receptor modification. Moreover, selective small-molecule inhibitors of DYRKs effectively suppressed IL-17RA phosphorylation at S801. Our findings indicate a link between DYRK family kinases and IL-17RA phosphorylation, providing new potential therapeutic targets in the management of IL-17-mediated diseases.
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