Dual specificity tyrosine phosphorylation regulated kinase 4 (DYRK4)

Dual specificity tyrosine phosphorylation regulated kinase 4 (DYRK4) is an enzyme in the DYRK protein kinase family, characterized by its ability to autophosphorylate on tyrosine and phosphorylate target substrates on serine/threonine residues[1][2][3]. DYRK4 is the least studied member of the five mammalian DYRK kinases. Its biological functions include regulation of cell differentiation, proliferation, and survival, with particularly restricted expression in testis and possible roles in reproductive tissue differentiation[1]. DYRK4 exhibits multiple splice variants with differential cellular localization, influencing functional capacities and enzymatic activity[1][2]. In neuronal cells, DYRK4 promotes dendritic branching, and in cancer models, it modulates cellular responses to DNA-damaging agents[1][2]. Its interaction with molecular chaperones like Hsp90 directly affects its stability and function[1]. While not currently a direct target for approved therapeutics, DYRK4’s involvement in cell differentiation and DNA damage response pathways makes it a research target in oncology and developmental biology[1][2][3][5].

Other names

Dual specificity tyrosine phosphorylation regulated kinase 4Dual specificity tyrosine-(Y)-phosphorylation regulated kinase 4Dual specificity tyrosine-phosphorylation-regulated kinase 4DYRK4Dyrk4DYRK4_HUMANEC 2.7.12.1[3][5]

Predicted mechanisms include kinase inhibition, especially targeting its dual specificity catalytic domain. Modulation of substrate phosphorylation and regulation of cellular localization for functional effects.