ArticleScientific reports2016
Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 26 citations in OpenAlex.
- Repetitive mild traumatic brain injury with the closed-head impact model of engineered rotational acceleration (CHIMERA) promotes tau pathology in tau transgenic mice and its propagation in brains injected with tau fibrils.Acta neuropathologica communications · 2026Article
- Novel aspects of the phosphorylation and structure of pathological tau: implications for tauopathy biomarkers.FEBS open bio · 2024Review
- Disease-Associated Mutations in Tau Encode for Changes in Aggregate Structure Conformation.ACS chemical neuroscience · 2023Article
- Phosphorylation mutation impairs the promoting effect of spastin on neurite outgrowth without affecting its microtubule severing ability.European journal of histochemistry : EJH · 2023Article
- Melatonin ameliorates tau-related pathology via the miR-504-3p and CDK5 axis in Alzheimer's disease.Translational neurodegeneration · 2022Article
- Defined Tau Phosphospecies Differentially Inhibit Fast Axonal Transport Through Activation of Two Independent Signaling Pathways.Frontiers in molecular neuroscience · 2020Article
- Tau isoform expression and phosphorylation in marmoset brains.The Journal of biological chemistry · 2019Article
- Isoform-independent and -dependent phosphorylation of microtubule-associated protein tau in mouse brain during postnatal development.The Journal of biological chemistry · 2018Article
- Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy.Frontiers in neuroscience · 2018Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is hyperphosphorylated in the brains of patients with tauopathies, such as Alzheimer's disease and frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). However, neither the mechanism of hyperphosphorylation nor its contribution to pathogenesis is known. We applied Phos-tag SDS-PAGE, a phosphoaffinity electrophoresis, to the analysis of tau phosphorylation in vitro by Cdk5, in cultured cells and in mouse brain. Here, we found that Cdk5-p25 phosphorylated tau in vitro at Ser404, Ser235, Thr205 and Ser202 in this order. In contrast in cultured cells, Ser404 was preferentially phosphorylated by Cdk5-p35, whereas Thr205 was not phosphorylated. Ser202 and Ser235 were phosphorylated by endogenous kinases. Tau exhibited ~12 phosphorylation isotypes in COS-7 cells with different combinations of phosphorylation at Thr181, Ser202, Thr231, Ser235 and Ser404. These phosphorylation sites were similar to tau phosphorylated in mouse brains. FTDP-17 tau with a mutation in the C-terminal region had different banding patterns, indicating a different phosphorylation pattern. In particular, it was clear that the R406W mutation causes loss of Ser404 phosphorylation. These results demonstrate the usefulness of the Phos-tag technique in the quantitative analysis of site-specific in vivo phosphorylation of tau and provide detailed information on in situ combinatory phosphorylation of tau.
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