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Hyperphosphorylation of tau leading to aggregated tau and tangle formation is acommon pathological feature of tauopathies, including Alzheimer's disease. Abnormalphosphorylation of tau by kinases, in particular GSK3ÃŽÂ², has been proposed as a pathogenicmechanism in these diseases. In this study we demonstrate that the heat shock protein 90(Hsp90) maintains the stability and function of the GSK3ÃŽÂ². By using both rat primarycortical neurons and COS-7 cells, we show that Hsp90 inhibitors lead to a reduction of theprotein level of GSK3ÃŽÂ², and that this effect is associated with both a decrease in tauphosphorylation at putative GSK3ÃŽÂ² sites and an induction in heat shock protein 70 (Hsp70)levels. We further show that Hsp90 associates with the GSK3ÃŽÂ² regulating its stability andfunction and preventing its degradation by the proteasome

Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β