Tau phosphorylation by GSK-3β promotes tangle-like filament morphology
2007
How GSK-3β Affects Tau Filaments in Alzheimer's Disease
publication
Evidence: moderate
Author Information
Author(s): Carolyn A Rankin, Qian Sun, Truman C Gamblin
Primary Institution: Department of Molecular Biosciences, University of Kansas, Lawrence, KS, USA
Hypothesis
GSK-3β is involved in some aspect of neurofibrillary tangle (NFT) formation.
Conclusion
Phosphorylation of tau by GSK-3β promotes the formation of tangle-like filament morphology.
Supporting Evidence
- Phosphorylation by GSK-3β is sufficient to cause tau filaments to coalesce into tangle-like aggregates.
- The study provides a new model system to study mechanisms of NFT development.
- Phosphorylation of tau alters the nature of interactions between filaments.
Takeaway
This study shows that a specific protein can help tau filaments clump together, which is important in diseases like Alzheimer's.
Methodology
In vitro cell-free model system to study tau phosphorylation and filament aggregation.
Limitations
The physiological relevance of using arachidonic acid as an inducer of tau polymerization is uncertain.
Statistical Information
P-Value
0.0142
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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