Mitogen-activated protein (MAP) kinases are a large class of proteins involved in signal transduction pathways that are activated by a range of stimuli and mediate a number of physiological and pathological changes in the cell. Dual specificity phosphatases (DSPs) are a subclass of the protein tyrosine phosphatase (PTP) gene superfamily, which are selective for dephosphorylating critical phosphothreonine and phosphotyrosine residues within MAP kinases. DSP gene expression is induced by a host of growth factors and/or cellular stresses, thereby negatively regulating MAP kinase superfamily members including MAPK/ERK, SAPK/JNK and p38. The members of the dual-specificity phosphatase protein family include MKP-1/CL100 (3CH134), VHR, PAC1, MKP-2, hVH-3 (B23), hVH-5, MKP-3, MKP-X, and MKP- 4. Human MKP-2 maps to chromosome 8p12-p11 and encodes a 394 amino acid, 43 kDa protein that specifically inactivates ERK1, ERK2 and JNK.