Dual-specificity tyrosine-regulated kinase (DYRK)

The dual-specificity tyrosine-regulated kinases (DYRKs) are a family of protein kinases within the CMGC group, characterized by the ability to phosphorylate substrates on serine/threonine as well as tyrosine residues. Humans encode five known DYRK proteins (DYRK1A, DYRK1B, DYRK2, DYRK3, DYRK4), all sharing a highly conserved catalytic core and structural domains specific to their class. DYRK kinases are pleiotropic regulators involved in critical cellular processes, including cell cycle regulation, developmental signaling, gene expression, DNA damage response, and the formation of specialized cellular structures such as the primary cilium. Dysregulation and mutation of these kinases are implicated in various diseases, notably some cancers, neurodevelopmental disorders, and other human pathologies. DYRKs are considered promising but challenging drug targets due to their central roles and the risk of off-target effects.

Other names

DYRK familyDYRK kinasesDual specificity tyrosine-phosphorylation-regulated kinase

Inhibition of kinase activity (ATP-competitive inhibition), regulation of substrate phosphorylation