Tau is a neuronal microtubule-associated protein whose function is modulated by phosphorylation. GSK-3beta is a tau kinase. GSK-3beta is part of the wingless signalling pathway and stimulation by wingless is predicted to down-regulate GSK-3beta 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-3beta-mediated phosphorylation of tau in transfected CHO cells. We find that co-transfection with dishevelled-1 is inhibitory to GSK-3beta-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
1997-07-14T00:00:00+00:00
411
369 - 372
3
Adaptor Proteins, Signal Transducing, Animals, Blotting, Western, CHO Cells, Calcium-Calmodulin-Dependent Protein Kinases, Cloning, Molecular, Cricetinae, Dishevelled Proteins, Drosophila, Drosophila Proteins, Gene Expression Regulation, Glycogen Synthase Kinase 3, Humans, Insect Proteins, Mice, Phosphoproteins, Phosphorylation, Signal Transduction, Transfection, tau Proteins