Protein phosphatases are a group of enzymes, found ubiquitously, which are responsible for the dephosphorylation of various proteins and enzymes in a cell. This role is an extremely important one since protein phosphorylation and dephosphorylation is required for the regulation of a large number of cellular activities.
Protein phosphatases were first reported to be inhibited by microcystins by Mackintosh et. al. (1990). It was found that extremely low concentrations of microcystin-LR could strongly inhibit protein phosphatases 1 and 2A from both plants and mammals, thereby causing hyperphosphorylation of the cell and a massive disruption of a number of important cellular mechanisms.
The binding of microcystins to protein phosphatases is covalent and therefore very inhibitory and highly specific. The processes involved in the binding of microcystins to protein phosphatases is the subject of some research.
Calcineurin subunit B type 2 is a protein that in humans is encoded by the PPP3R2 gene.
Protein phosphatase 2 (PP2), also known as PP2A, is an enzyme that in humans is encoded by the PPP2CA gene. The PP2A heterotrimeric protein phosphatase, is a ubiquitous and conserved Serine/Threonine phosphatase with broad substrate specificity and diverse cellular functions. Among the targets of PP2A are proteins of oncogenic signaling cascades, such as Raf, MEK, and AKT.
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