Syk Tyrosine Kinase Phosphorylates Tau Protein
Author Information
Author(s): Lebouvier Thibaud, Scales Timothy M.E., Hanger Diane P., Geahlen Robert L., Lardeux Bernard, Reynolds C. Hugh, Anderton Brian H., Derkinderen Pascal
Primary Institution: Inserm, U643, Nantes, France
Hypothesis
Can Syk tyrosine kinase phosphorylate tau protein?
Conclusion
Syk is identified as a tyrosine kinase that phosphorylates tau, particularly at tyrosine 18, which may have implications for neurodegenerative disorders.
Supporting Evidence
- Syk can phosphorylate tau in vitro and in CHO cells.
- Tyrosine 18 is identified as the primary phosphorylation site for Syk on tau.
- Syk binds to tau, indicating a direct interaction between the two proteins.
Takeaway
This study found that a protein called Syk can add a special tag to another protein called tau, which is important for understanding brain diseases.
Methodology
The study used in vitro phosphorylation assays and co-transfection experiments in CHO cells to investigate the interaction between Syk and tau.
Digital Object Identifier (DOI)
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