ArticleJournal of neural transmission (Vienna, Austria : 1996)2006
PP2B isolated from human brain preferentially dephosphorylates Ser-262 and Ser-396 of the Alzheimer disease abnormally hyperphosphorylated tau.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Tau protein in Parkinson's disease: advances in phosphoproteomics and molecular dynamics simulations.Frontiers in aging neuroscience · 2026Review
- Tauopathies: Calmodulin Regulates Tau Hyperphosphorylation and Its Transformation into Disease-Specific Aggregates.Biomolecules · 2025Review
- Role of saturated fatty acid metabolism in posttranslational modifications of the Tau protein.Molecular and cellular biochemistry · 2025Review
- Molecular mechanisms and consequences of TDP-43 phosphorylation in neurodegeneration.Molecular neurodegeneration · 2025Review
- Single-cell transcriptomic and neuropathologic analysis reveals dysregulation of the integrated stress response in progressive supranuclear palsy.Acta neuropathologica · 2024Article
- Updates in Alzheimer's disease: from basic research to diagnosis and therapies.Translational neurodegeneration · 2024Review
- Cytomegalovirus infection induces Alzheimer's disease-associated alterations in tau.Journal of neurovirology · 2023Article
- Chronic Presence of Oligomeric Aβ Differentially Modulates Spine Parameters in the Hippocampus and Cortex of Mice With Low APP Transgene Expression.Frontiers in synaptic neuroscience · 2020Article
- Ageing and amyloidosis underlie the molecular and pathological alterations of tau in a mouse model of familial Alzheimer's disease.Scientific reports · 2019Article
- Protein Phosphatase 2A and Its Methylation Modulating Enzymes LCMT-1 and PME-1 Are Dysregulated in Tauopathies of Progressive Supranuclear Palsy and Alzheimer Disease.Journal of neuropathology and experimental neurology · 2018Article
- Transcriptome analyses of chronic traumatic encephalopathy show alterations in protein phosphatase expression associated with tauopathy.Experimental & molecular medicine · 2017Article
- Region-specific dendritic simplification induced by Aβ, mediated by tau via dysregulation of microtubule dynamics: a mechanistic distinct event from other neurodegenerative processes.Molecular neurodegeneration · 2015Article
- Calmodulin Binding Proteins and Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2015Article
- Tau protein modifications and interactions: their role in function and dysfunction.International journal of molecular sciences · 2014Review
- Phosphatases of α-synuclein, LRRK2, and tau: important players in the phosphorylation-dependent pathology of Parkinsonism.Frontiers in genetics · 2014Review
- Calcineurin regulation of cytoskeleton organization: a new paradigm to analyse the effects of calcineurin inhibitors on the kidney.Journal of cellular and molecular medicine · 2012Review
- Unveiling clusters of RNA transcript pairs associated with markers of Alzheimer's disease progression.PloS one · 2012Article
- Protein phosphatases and Alzheimer's disease.Progress in molecular biology and translational science · 2012Review
- A role for calcineurin in Alzheimer's disease.Current neuropharmacology · 2011Article
- Transcriptomic analysis of human retinal detachment reveals both inflammatory response and photoreceptor death.PloS one · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
PP2B is one of the major serine/threonine phosphatases in the brain. We quantitated the dephosphorylation of various sites of Alzheimer disease abnormally hyperphosphorylated tau by PP2B purified from six (three Alzheimer and three control) autopsied human brains. The purified PP2B was essentially homogenous holoenzyme as determined by SDS-PAGE, Western blot analyses and biochemical characterization. Purified PP2B from all six brains efficiently dephosphorylated (32)P-tau with specific activities ranging from 684-1286 pmol (32)Pi/mg/min. Estimated by dot-blot analyses, the purified PP2B (on average from six brains) dephosphorylated Alzheimer tau at pS199, pT217, pS262, pS396 and pS422 by 38%, 32%, 63%, 78%, and 32%, respectively. Dephosphorylation of tau at pT181, pS202, pT205, pT212, pS214, and pS404 by PP2B was undetectable. The preferential dephosphorylation of Ser262 and Ser396 by PP2B suggests a possible involvement of this phosphatase in Alzheimer neurofibrillary degeneration.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.