Dual specificity phosphatase 18 (DUSP18)

Dual specificity phosphatase 18 (DUSP18) is an atypical dual specificity phosphatase enzyme that dephosphorylates both tyrosine and serine/threonine residues on substrate proteins[1][2][7]. It is a member of the protein tyrosine phosphatase (PTP) family, classified under the cysteine-based PTPs, and is considered "atypical" due to lack of the N-terminal CH2 domain found in mitogen-activated protein kinase phosphatases (MKPs)[1][6][7]. Structurally, DUSP18 contains a C-terminal DUSP catalytic domain and has unique substrate specificity and thermostability features[2]. Functionally, DUSP18 has key roles in cell signaling—regulating MAPK14 (p38 MAPK) activity, modulating cholesterol biosynthesis via control of the SREBF2 pathway, and promoting malignant phenotypes such as proliferation, migration, and invasion in certain cancers including hepatocellular and colorectal carcinoma[4][5]. No clinically approved drugs are known to target DUSP18 directly, but its roles in cancer cell biology and metabolism make it a potential therapeutic target.

Other names

Dual specificity protein phosphatase 18DUSP18LMWDSP20LMW-DSP20DUSP20Low molecular weight dual specificity phosphatase 20DSP18

Catalyzes dephosphorylation of tyrosine and serine/threonine residues on target proteins, especially within MAPK pathways