Protein phosphatase 2A is a heterotrimeric protein serine/threonine phosphatase consisting of a 36-kD catalytic C subunit (alpha and beta isoforms), a 65-kD structural A subunit (alpha and beta isoforms), and a variable regulatory B subunit. When the PP2A catalytic C subunit associates with the A and B subunits several species of holoenzymes are produced with distinct functions and characteristics. Ubiquitously expressed, PP2A is involved in a broad range of cellular processes, including membrane receptor desensitization, signal transduction, intermediary metabolism, transcriptional regulation and control of DNA replication, and mitosis. The PP2A phosphatase family accounts for the majority of Ser/Thr phosphatase activity in the brain and specifically regulates tau phosphorylation, both directly as tau phosphatase and indirectly by regulating the activities of several tau kinases which include CaM Kinase II, PKA, MAP kinase kinase (MEK 1/2), extracellular regulated kinase (ERK 1/2), GSK-3β, and P70S6 kinase, thus regulating tau microtubule binding in the brain. When PP2A B' delta (PP2A 56 kDa regulatory subunit delta isoform) is associated with the A and C subunits, tau protein cannot bind to PP2A and be dephosphorylated, leading to increased tau aggregation.
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