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

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

* ,  and
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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Abstract: 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.
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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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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.

AMA Style

Dou F, Chang X, Ma D. Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β. International Journal of Molecular Sciences. 2007; 8(1):51-60.

Chicago/Turabian Style

Dou, Fei; Chang, Xingya; Ma, Da. 2007. "Hsp90 Maintains the Stability and Function of the Tau Phosphorylating Kinase GSK3β." Int. J. Mol. Sci. 8, no. 1: 51-60.



Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert