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. MKP-5 preferentially binds to p38, but also to SAPK/JNK. It is ubiquitously expressed and localizes to both the cytoplasm and the nucleus. MKP-5 has been implicated in cell proliferation and apoptosis, tumor invasion and immune responses.
