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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.

Type

Journal article

Journal

FEBS Lett

Publication Date

14/07/1997

Volume

411

Pages

369 - 372

Keywords

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