DUSP5 (dual specificity phosphatase 5) is a dual-specificity protein phosphatase that dephosphorylates both serine/threonine and tyrosine residues, with highest activity toward ERK1 1. The enzyme functions as a negative regulator of MAPK signaling pathways, particularly the ERK1/2 cascade, by dephosphorylating and inactivating these kinases 23. DUSP5 expression is regulated by post-translational modifications, with ubiquitination leading to its degradation 4. The protein demonstrates context-dependent roles in disease pathogenesis. In cancer, DUSP5 is upregulated in lung adenocarcinoma, particularly in KRAS-mutant tumors, where it promotes cell proliferation and poor survival outcomes 5. Conversely, DUSP5 exhibits protective functions in inflammatory conditions: it suppresses IL-1β-induced chondrocyte inflammation in osteoarthritis by inhibiting NF-κB and ERK pathways 3, and its knockdown in acute kidney injury enhances autophagy through AMPK/ULK1 signaling, reducing inflammation and apoptosis 6. In chr10 prostatitis, epithelial cell-derived exosomal miR-203a-3p targets DUSP5, promoting stromal inflammation via ERK1/2/MCP-1 signaling 2. DUSP5 represents a potential therapeutic target, with its modulation showing promise in treating various pathological conditions including autoimmune diseases and cancer 7.