Tyrosine-protein kinase RYK (RYK)

Tyrosine-protein kinase RYK (RYK) is an atypical, catalytically inactive transmembrane receptor of the receptor tyrosine kinase family, with structural similarity to growth factor receptors but lacking kinase activity due to key residue substitutions in the activation domain[1][2][3]. It contains an extracellular Wnt inhibitory factor (WIF)-type ligand-binding domain and is mainly considered a receptor or co-receptor for Wnt ligands, acting through canonical (β-catenin dependent) and non-canonical signaling pathways[1][2][3]. RYK participates in a wide range of developmental processes, particularly axon guidance and neural patterning, and modulates actin cytoskeleton dynamics and cell polarity; aberrant RYK signaling has been implicated in tumor progression (promoting cancer stem cell properties and invasiveness) and developmental disorders[1][2][3]. Its function is thought to depend on recruitment of signaling partners, receptor cleavage and nuclear translocation of fragments, and modulation of other Wnt pathway components rather than direct enzymatic phosphorylation[1][3].

Other names

RYKJTK5JTK5ARYK1D3S3195Tyrosine-protein kinase RYKHydroxyaryl-protein kinase

Modulation of Wnt ligand-receptor interactions. Regulation of downstream Wnt/β-catenin signaling. Protein–protein interaction signaling (without intrinsic kinase activity).