Tau is a neuronal microtubule‐associated protein whose function is modulated by phosphorylation. GSK‐3β is a tau kinase. GSK‐3β is part of the wingless signalling pathway and stimulation by wingless is predicted to down‐regulate GSK‐3β activity. In Drosophila imaginal disc cells, overexpression of dishevelled, a component of the wingless pathway, mimics the wingless signal. We have therefore studied the effect that overexpression of the murine dishevelled‐1 protein has on GSK‐3β‐mediated phosphorylation of tau in transfected CHO cells. We find that co‐transfection with dishevelled‐1 is inhibitory to GSK‐3β‐mediated tau phosphorylation. Tau is hyperphosphorylated in Alzheimer's disease and the possible relevance of these findings to Alzheimer's disease pathogenesis are discussed.
Journal article
Wiley
1997-07-14T00:00:00+00:00
411
369 - 372
3