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Localization, induction, and cellular effects of tau-phospho-threonine 217

Binita Rajbanshi, James W. Mandell, View ORCID ProfileGeorge S. Bloom
doi: https://doi.org/10.1101/2022.04.18.488657
Binita Rajbanshi
aDepartment of Pharmacology, University of Virginia, Charlottesville, VA, USA
bDepartment of Biology, University of Virginia, Charlottesville, VA, USA
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James W. Mandell
cDepartment of Pathology, University of Virginia, Charlottesville, VA, USA
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George S. Bloom
bDepartment of Biology, University of Virginia, Charlottesville, VA, USA
dDepartment of Cell Biology, University of Virginia, Charlottesville, VA, USA
eDepartment of Neuroscience, University of Virginia, Charlottesville, VA, USA
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  • ORCID record for George S. Bloom
  • For correspondence: gsb4g@virginia.edu
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ABSTRACT

Introduction Tau phosphorylation at T217 is a promising AD biomarker, but its functional consequences were unknown.

Methods Human brain and cultured mouse neurons were analyzed by immunoblotting and immunofluorescence for total tau, taupT217, taupT181, taupT231 and taupS396/pS404. dSTORM super resolution microscopy was used to localize taupT217 in cultured neurons. EGFP-tau was expressed in fibroblasts as wild type and T217E pseudo-phosphorylated tau, and fluorescence recovery after photobleaching (FRAP) reported tau turnover rates on microtubules.

Results In brain, taupT217 appears in neurons at Braak stages I-II, becomes more prevalent later and co-localizes partially with other phospho-tau epitopes. In cultured neurons taupT217, is increased by extracellular tau oligomers (xcTauOs), and is associated with developing post-synaptic sites. FRAP recovery was fastest for EGFP-tauT217E.

Conclusion TaupT217 increases in brain as AD progresses and is induced by xcTauOs. Post-synaptic taupT217 suggests a role for T217 phosphorylation in synapse impairment. T217 phosphorylation reduces tau’s affinity for microtubules.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted April 18, 2022.
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Localization, induction, and cellular effects of tau-phospho-threonine 217
Binita Rajbanshi, James W. Mandell, George S. Bloom
bioRxiv 2022.04.18.488657; doi: https://doi.org/10.1101/2022.04.18.488657
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Localization, induction, and cellular effects of tau-phospho-threonine 217
Binita Rajbanshi, James W. Mandell, George S. Bloom
bioRxiv 2022.04.18.488657; doi: https://doi.org/10.1101/2022.04.18.488657

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