Journal article

GSK-3 beta dysregulation contributes to parkinson's-like pathophysiology with associated region-specific phosphorylation and accumulation of tau and alpha-synuclein

JJ Credle, JL George, J Wills, V Duka, K Shah, Y-C Lee, O Rodriguez, T Simkins, M Winter, D Moechars, T Steckler, J Goudreau, DI Finkelstein, A Sidhu

CELL DEATH AND DIFFERENTIATION | NATURE PUBLISHING GROUP | Published : 2015

Abstract

Aberrant posttranslational modifications (PTMs) of proteins, namely phosphorylation, induce abnormalities in the biological properties of recipient proteins, underlying neurological diseases including Parkinson's disease (PD). Genome-wide studies link genes encoding α-synuclein (α-Syn) and Tau as two of the most important in the genesis of PD. Although several kinases are known to phosphorylate α-Syn and Tau, we focused our analysis on GSK-3β because of its accepted role in phosphorylating Tau and to increasing evidence supporting a strong biophysical relationship between α-Syn and Tau in PD. Therefore, we investigated transgenic mice, which express a point mutant (S9A) of human GSK-3β. GSK-..

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