DUSP2 is a dual-specificity phosphatase that dephosphorylates both phosphorylated threonine and tyrosine residues on mitogen-activated protein kinases (MAPKs), particularly MAPK1, with slightly faster activity on phosphotyrosine. This phosphatase activity positions DUSP2 as a negative regulator of MAPK signaling cascades including ERK and p38 pathways. In cancer contexts, DUSP2 functions as a tumor suppressor. In gastric cancer, DUSP2 suppression via exosomal miR-519a-3p promotes liver metastasis by activating MAPK/ERK signaling in intrahepatic macrophages 1. In pancreatic cancer, DUSP2 promotes apoptosis under hypoxic conditions through an ERK1/2-independent mechanism involving recruitment of casein kinase 2 alpha 1 to suppress AKT1 phosphorylation 2. Conversely, in nasopharyngeal carcinoma, DNTTIP1-mediated suppression of DUSP2 via histone deacetylase 1 recruitment leads to aberrant ERK activation and increased metastatic potential 3. In bladder cancer, DUSP2 overexpression inhibits proliferation and metastasis by downregulating MEK/ERK and p38 MAPK signaling 4. Beyond cancer, DUSP2 protects renal tubular epithelial cells by inactivating STAT1 to prevent gasdermin D-mediated pyroptosis in acute kidney injury 5. DUSP2 is also dysregulated in autoimmune contexts, implicated in systemic lupus erythematosus pathogenesis. These findings suggest DUSP2 modulation—either inhibition or restoration depending on disease context—as a therapeutic target.