AUTHOR=Sontag Jean-Marie , Sontag Estelle TITLE=Protein phosphatase 2A dysfunction in Alzheimer’s disease JOURNAL=Frontiers in Molecular Neuroscience VOLUME=7 YEAR=2014 URL=https://www.frontiersin.org/journals/molecular-neuroscience/articles/10.3389/fnmol.2014.00016 DOI=10.3389/fnmol.2014.00016 ISSN=1662-5099 ABSTRACT=
Protein phosphatase 2A (PP2A) is a large family of enzymes that account for the majority of brain Ser/Thr phosphatase activity. While PP2A enzymes collectively modulate most cellular processes, sophisticated regulatory mechanisms are ultimately responsible for ensuring isoform-specific substrate specificity. Of particular interest to the Alzheimer’s disease (AD) field, alterations in PP2A regulators and PP2A catalytic activity, subunit expression, methylation and/or phosphorylation, have been reported in AD-affected brain regions. “PP2A” dysfunction has been linked to tau hyperphosphorylation, amyloidogenesis and synaptic deficits that are pathological hallmarks of this neurodegenerative disorder. Deregulation of PP2A enzymes also affects the activity of many Ser/Thr protein kinases implicated in AD. This review will more specifically discuss the role of the PP2A/Bα holoenzyme and PP2A methylation in AD pathogenesis. The PP2A/Bα isoform binds to tau and is the primary tau phosphatase. Its deregulation correlates with increased tau phosphorylation