Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A
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A new paradigm for regulation of protein phosphatase 2A function via Src and Fyn kinase–mediated tyrosine phosphorylation
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2019, Advances in Cancer ResearchCitation Excerpt :In the pathology of Alzheimer's disease (AD) and other related neurodegenerative diseases called tauopathies, Tau protein is abnormally hyperphosphorylated, which results in its aggregation into filament bundles (Grundke-Iqbal et al., 1986). This observation led to the discovery of PP2A as a key mediator of Tau dephosphorylation in the brain and implicated its inactivity in tauopathy disease progression (Drewes et al., 1993; Gong et al., 1994). Using highly purified and recombinant proteins in in vitro dephosphorylation assays as well as structure-guided mutagenesis, the molecular basis for Tau binding to PP2A/B55α has become more clearly understood.
The protein serine/threonine phosphatases PP2A, PP1 and calcineurin: A triple threat in the regulation of the neuronal cytoskeleton
2017, Molecular and Cellular Neuroscience
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