Substrate-specific reduction of PP2A activity exaggerates tau pathology

Deters, Natasha; Ittner, Lars M.; Götz, Jürgen

doi:10.1016/j.bbrc.2008.12.140

Cited by 40Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchAldose Reductase and Taurine

Substrate-specific reduction of PP2A activity exaggerates tau pathology

Deters, Natasha, Ittner, Lars M., Götz, Jürgen·2009·Biochemical and Biophysical Research Communications

DOI 10.1016/j.bbrc.2008.12.140

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Abstract

Phosphorylation of the microtubule-associated protein tau is regulated by the balanced interplay of kinases and phosphatases. Disturbance of this balance causes hyperphosphorylation of tau and neurofibrillary tangle formation in Alzheimer's disease brain. Here, we crossed Dom5 mice that express a substrate-specific dominant negative mutant form, L309A Calpha, of protein phosphatase 2A (PP2A) with neurofibrillary-tangle-forming P301L mutant tau transgenic pR5 mice. This exacerbated the tau pathology of pR5 mice significantly. Double-transgenic Dom5/pR5 mice showed 7-fold increased numbers of hippocampal neurons that specifically phosphorylated the pathological S422 epitope of tau. They showed 8-fold increased numbers of tangles compared to pR5 mice, in agreement with our previous finding that tangle formation is correlated with and preceded by phosphorylation of tau at the S422 epitope. This suggests that, in addition to kinases, PP2A and its regulatory subunits may be a therapeutic target for Alzheimer's disease.

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Crossbreeding of these mice with P301L mutant tau transgenic pR5 mice intensified tau pathology, further increasing tau Ser422 phosphorylation and neurofibrillary tangle formation in hippocampus and amygdala.
“Interestingly, crossbreeding of these mice with P301L mutant tau transgenic pR5 mice intensified the tau pathology, further increasing tau Ser422 phosphorylation and neurofibrillary tangle (NFT) formation in hippocampus and amygdala [50].”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [50]

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Authors: Deters, N., Ittner, L. M., & Götz, J.
Affiliations: The University of Sydney (AU)
Corresponding author: Götz, Jürgen
ORCID: Ittner, Lars M.
Götz, Jürgen
Venue: Biochemical and Biophysical Research Communications
Publisher: Elsevier BV
Published: 2009-02
Volume: 379
Issue: 2
Pages: 400-405
ISSN: 0006-291X (ISSN-L)
DOI: 10.1016/j.bbrc.2008.12.140
OpenAlex: W2060082076
Cited by: 39
References: 30
Citations by year: 2025: 2 · 2022: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 1 · 2014: 1 · 2013: 6 · 2012: 7
FWCI: 4.42
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biochemical and Biophysical Research Communications (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
Keywords: protein phosphatase 2A, tau hyperphosphorylation, neurofibrillary tangles, Alzheimer's disease, PP2A regulatory subunit, tau phosphorylation, hippocampal neurons, therapeutic target
MeSH terms: Alzheimer Disease, Animals, Brain, Humans, Mice, Transgenic, Mutation, Phosphorylation, Solubility, Substrate Specificity, Neurofibrillary Tangles, tau Proteins, Protein Subunits, Mice, Protein Phosphatase 2

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Substrate-specific reduction of PP2A activity exaggerates tau pathology

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