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Beschreibung

Serine/threonine-protein phosphatase 2A catalytic subunit alpha/beta isoforms (UniProt: P67775/P62714, also known as EC 3.1.3.16, PP2A-alpha/PP2A-beta) is encoded by the PPP2CA/PPP2CB gene (Gene ID: 5515/5516) in human. Protein phosphatase 2A (PP2A) is a ubiquitously expressed enzyme that contributes 0.3 to 1% of the total cellular protein in the mammalian cell and regulates various functions by dephosphorylating many critical molecules, such as Akt, p53, c-Myc, CK2, S6 kinase, and beta-catenin. It is the major phosphatase for microtubule-associated proteins (MAPs). PP2A acts as a pivotal cellular switch controlling important events in cell, such as cell cycle, apoptosis, and autophagy It suppresses mitogenic signals and is suggested as a tumor suppressor. Aberrant expression and mutations in the PP2AA and PP2AB subunits are reported in various human malignancies. PP2A is made up of a functional heterotrimeric complex, which includes a structural subunit (PP2AA), a regulatory subunit (PP2AB), and a catalytic subunit (PP2AC). The regulatory subunit determines its substrate specificity. Over 20 different interchangeable regulatory subunits have been described that allows it to act on a large number of substrates. PP2AC has multiple metal ion binding sites and binds two manganese ions per subunit. Two isoforms of PP2AC (alpha and beta) have been described that display high degree of homology. PP2AC alpha also has two isoforms (PP2AC alpha 1 and alpha 2). The PP2AC alpha 2 isoform is shown to be catalytically inactive because it lacks amino acids 193-246.