In recent years a heightened appreciation has emerged for the role(s) that phosphatases play in regulating signal transduction pathways and other cellular processes. The tumor-promoting agent okadaic acid (OA) has been an invaluable tool in efforts aimed at delineating the contributions of the most abundant mammalian serine/threonine phosphatase, protein phosphatase 2A (PP2A), to intracellular signaling and cell function. PP2A, which is ubiquitous and vital in virtually every cell system studied, continues to be the focus of much research on phosphorylation control machinery. Mast cells represent an excellent in vitro model for the study of protein phosphorylation events because they possess a number of distinct signaling pathways that lead to the production and/or release of discreet mediators in response to different stimuli. The utility of OA in analyzing PP2A function has been demonstrated in mast cells across several species. Results of these studies have contributed to the current recognition that PP2A plays a crucial role in the biology of mast cells and other cell types.