ArticleSerican journal of medicine2026
DYRK kinases phosphorylate IL-17RA at S801.
Article in Serican journal of medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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