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Overview
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Background
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. DUSP22 dephosphorylates ERK2 MAP kinase and JNK. DUSP22 displays highest in thymus, but it is also detectable in monocytes and lymphocytes.
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