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Int. J. Mol. Sci. 2007, 8(1), 51-60; doi:10.3390/i8010060

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

Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Southeast University Medical School, Nanjing 210009, P.R.China
Author to whom correspondence should be addressed.
Received: 2 January 2007 / Accepted: 23 January 2007 / Published: 30 January 2007
(This article belongs to the Special Issue Interaction of Biological Molecules)
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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 GSK3β, 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 GSK3β. By using both rat primarycortical neurons and COS-7 cells, we show that Hsp90 inhibitors lead to a reduction of theprotein level of GSK3β, and that this effect is associated with both a decrease in tauphosphorylation at putative GSK3β sites and an induction in heat shock protein 70 (Hsp70)levels. We further show that Hsp90 associates with the GSK3β regulating its stability andfunction and preventing its degradation by the proteasome. View Full-Text
Keywords: tauopathy; GSK3β; Hsp90; aberrant tau phosphorylation tauopathy; GSK3β; Hsp90; aberrant tau phosphorylation

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Dou, F.; Chang, X.; Ma, D. Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β. Int. J. Mol. Sci. 2007, 8, 51-60.

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