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Updated: May 8, 2026
12:47
Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins
Published on: December 27, 2016
How it all started: tau and protein phosphatase 2A.
1Brain and Mind Research Institute, University of Sydney, Camperdown, NSW, Australia.
Journal of Alzheimer'S Disease : JAD
|August 17, 2013
Summary
This review honors Inge Grundke-Iqbal
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- The review honors Inge Grundke-Iqbal's foundational work on tau pathology in Alzheimer's disease (AD).
- Key discoveries include tau isolation from AD brains, identification of tau hyperphosphorylation, and the role of protein phosphatase 2A (PP2A) and its inhibitor I2PP2A.
Purpose of the Study:
- To review the critical role of PP2A and its inhibitor in tau phosphorylation.
- To discuss the impact of methylation and phosphorylation on PP2A activity.
- To present contributions to understanding tau and PP2A in AD using genetic models and explore underexplored areas in tau research.
Main Methods:
- Subcellular fractionation techniques for tau isolation.
- Review of biochemical mechanisms involving PP2A and I2PP2A in tau phosphorylation.
- Utilizing PP2A transgenic and knockout models to study tau and PP2A in Alzheimer's disease.
Main Results:
- Detailed review of PP2A and I2PP2A's role in tau phosphorylation.
- Discussion on how methylation and phosphorylation regulate PP2A activity.
- Insights from genetic models on tau and PP2A involvement in AD pathogenesis.
Conclusions:
- The review highlights the significance of PP2A and its inhibitor in tau phosphorylation and AD.
- It emphasizes the need to explore tau's non-canonical functions and the physiological roles of distinct tau isoforms.
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