ArticleNeurochemical research2005
Phosphothreonine-212 of Alzheimer abnormally hyperphosphorylated tau is a preferred substrate of protein phosphatase-1.
Article in Neurochemical research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Plasma p-tau212 identifies cognitively unimpaired individuals with emerging amyloid-β pathology.Journal of neurology · 2025Article
- Role of saturated fatty acid metabolism in posttranslational modifications of the Tau protein.Molecular and cellular biochemistry · 2025Review
- Plasma p-tau212 as a biomarker of sporadic and Down syndrome Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Updates in Alzheimer's disease: from basic research to diagnosis and therapies.Translational neurodegeneration · 2024Review
- Sut-6/NIPP1 modulates tau toxicity.Human molecular genetics · 2023Article
- Phosphomimetics at Ser199/Ser202/Thr205 in Tau Impairs Axonal Transport in Rat Hippocampal Neurons.Molecular neurobiology · 2023Article
- Zinc in Regulating Protein Kinases and Phosphatases in Neurodegenerative Diseases.Biomolecules · 2022Review
- Frontotemporal Lobar Dementia Mutant Tau Impairs Axonal Transport through a Protein Phosphatase 1γ-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Hippocampal tau oligomerization early in tau pathology coincides with a transient alteration of mitochondrial homeostasis and DNA repair in a mouse model of tauopathy.Acta neuropathologica communications · 2020Article
- Targeting Tau to Treat Clinical Features of Huntington's Disease.Frontiers in neurology · 2020Review
- Tau in neurodegenerative disease.Annals of translational medicine · 2018Review
- Biological function of Lemur tyrosine kinase 2 (LMTK2): implications in neurodegeneration.Molecular brain · 2018Review
- 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
- Aβ Influences Cytoskeletal Signaling Cascades with Consequences to Alzheimer's Disease.Molecular neurobiology · 2015Review
- Molecular and cellular mechanism of okadaic acid (OKA)-induced neurotoxicity: a novel tool for Alzheimer's disease therapeutic application.Molecular neurobiology · 2014Review
- 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
- Protein phosphatases and Alzheimer's disease.Progress in molecular biology and translational science · 2012Review
- Unveiling clusters of RNA transcript pairs associated with markers of Alzheimer's disease progression.PloS one · 2012Article
- Tau and tauopathies.Progress in molecular biology and translational science · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We isolated and characterized several phosphoseryl/phosphothreonyl phosphatase activities (P1-P11) from frontal lobe of six autopsied human brains. Of these, PP1 (P3) was a major tau phosphatase. The enzyme required metal ions and was maximally activated by Mn2+. Western blots with antibodies to known protein phosphatases showed PP1 and PP2B immunoreactivity. However, the removal of PP2B by immunoabsorption or its inhibition with EGTA did not result in appreciable loss of P3 activity. These observations suggest that P3 was an enriched PPI. Dephosphorylation of Alzheimer disease hyperphosphorylated tau (AD P-tau) by PP1 was site-specific. PPI preferentially dephosphorylated pT212 (40%), pT217 (26%), pS262 (33%), pS396 (42%) and pS422 (31%) of AD P-tau. Dephosphorylation of tau at pT181, pS199, pS202, pT205, pS214, and pS404, was undetectable. Of the sites dephosphorylated, pT212 was only a substrate for PP1, as purified/enriched PP2A and PP2B from the same brains did not dephosphorylate this site.
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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.