Dual specificity protein phosphatase 23 (DUSP23)

Dual specificity protein phosphatase 23 (DUSP23) is a small (≈150–amino acid) enzyme that catalyzes the dephosphorylation of both phosphotyrosine and phosphoserine/threonine residues on substrate proteins. DUSP23 localizes predominantly to the cytoplasm and centrosome, where it regulates G1/S cell cycle progression, cell proliferation, and cell–cell adhesion by dephosphorylating β-catenin at Tyr142, thereby strengthening α–/β–catenin interactions and stabilizing E-cadherin–mediated adherens junctions. It is structurally classified as the smallest catalytically active dual specificity phosphatase and plays roles in signaling pathways relevant to tumorigenesis, angiogenesis, and epithelial tissue homeostasis.

Other names

DUSP23DUSP25LDP-3LDP3VHZMOSPVH1-like phosphatase Zlow molecular mass dual specificity phosphatase 3testicular tissue protein Li 59FLJ20442

Drugs targeting DUSP23 would function as phosphatase modulators, altering dephosphorylation of key signaling proteins such as ERK1, JNK, p38, and β-catenin