Dual specificity protein phosphatase 2 (DUSP2)

Dual specificity protein phosphatase 2 (DUSP2), also known as PAC1 or PAC-1, is an enzyme that dephosphorylates both phosphoserine/threonine and phosphotyrosine residues on mitogen-activated protein kinases (MAPKs), primarily ERK1 and ERK2[1][2][3]. This activity places DUSP2 as a negative regulator of MAPK-dependent signaling pathways involved in cellular proliferation, differentiation, and survival[1][2][3]. Predominantly expressed in hematopoietic tissues and localized to the nucleus, DUSP2 is implicated in apoptosis, immune regulation, and tumor suppression, including the control of proinflammatory pathways. Genetic mutations and altered expression of DUSP2 have been associated with hematologic malignancies and resistance to therapy in various cancers, and it acts as an immune checkpoint in exhausted tumor-infiltrating lymphocytes. Due to its central role in negative regulation of MAPK signaling, DUSP2 represents an emerging potential therapeutic target for cancer and immune-mediated diseases[1][3].

Other names

PAC1PAC-1Dual specificity phosphatase 2Dual specificity protein phosphatase PAC-1serine/threonine specific protein phosphatase

Drugs or molecules targeting DUSP2 would act by modulating the dephosphorylation (inactivation) of MAP kinases, thereby influencing cellular proliferation, differentiation, and inflammatory responses[2][3][4].