The involvement of glycogen synthase kinase-3 and protein phosphatase-2A in lactacystin-induced tau accumulation

FEBS Letters
Qing-Guo RenJian-Zhi Wang

Abstract

Here, we demonstrated that lactacystin inhibited proteasome dose-dependently in HEK293 cells stably expressing tau. Simultaneously, it induces accumulation of both non-phosphorylated and hyperphosphorylated tau and decreases the binding of tau to the taxol-stabilized microtubules. Lactacystin activates glycogen synthase kinsase-3 (GSK-3) and decreases the phosphorylation of GSK-3 at serine-9. LiCl inhibits GSK-3 and thus reverses the lactacystin-induced accumulation of the phosphorylated tau. Lactacystin also inhibits protein phosphase-2A (PP-2A) and it significantly increases the level of inhibitor 1 of PP-2A. These results suggest that inhibition of proteasome by lactacystin induces tau accumulation and activation of GSK-3 and inhibition of PP-2A are involved.

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Citations

Mar 1, 2012·Molecular Neurobiology·Tobias MoraweChristian Behl
Dec 11, 2013·Journal of Molecular Neuroscience : MN·Min XieXiao-Mei Liao
Nov 26, 2013·Molecular and Cellular Neurosciences·Lotta AgholmeMartin Hallbeck
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May 5, 2009·Pathophysiology : the Official Journal of the International Society for Pathophysiology·Yao ZhangJian-Zhi Wang
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