Role of PP2A and Pin1 in Tau Phosphorylation in Alzheimer's Disease
Author Information
Author(s): Isabelle Landrieu, Caroline Smet-Nocca, Laziza Amniai, Justin Vijay Louis, Jean-Michel Wieruszeski, Jozef Goris, Veerle Janssens, Guy Lippens
Primary Institution: CNRS-UMR 8576, University of Lille-North of France
Hypothesis
Does the phosphorylation of Tau at specific sites influence its dephosphorylation by PP2A and the regulatory role of Pin1?
Conclusion
Phosphorylation of T231 negatively affects the dephosphorylation of pS202/pT205, and this interaction is regulated by Pin1.
Supporting Evidence
- PP2A is a major phosphatase that dephosphorylates Tau.
- Phosphorylation at T231 negatively interferes with dephosphorylation at S202/T205.
- Pin1 can release the negative feedback on Tau dephosphorylation.
Takeaway
This study shows that certain parts of a protein called Tau can affect how it gets changed back to its original form, which is important in Alzheimer's disease.
Methodology
NMR spectroscopy was used to analyze the dephosphorylation rates of phospho-Tau by PP2A.
Digital Object Identifier (DOI)
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