Ye Feng, Yiyuan Xia, Guang Yu, Xiji Shu, Haoliang Ge, Kuan Zeng, Jianzhi Wang and Xiaochuan Wang Cleavage of GSK-3β by calpain counteracts the inhibitory effect of Ser9 phosphorylation on GSK-3β activity induced by H2O2 Journal of Neurochemistry 126
GSK-3β dysfunction is critical in the pathogenesis of psychiatric, metabolic, neurodegenerative diseases, in which oxidative stress exists concurrently. Under H2O2 condition, Akt (also known as Protein Kinase B, PKB) activation increases phospho-Ser9 of glycogen synthase kinase (GSK)-3β, an inactivated form of GSK-3β. Simultaneously, calpain activation leads to GSK-3β truncation, which in turn overrides the inhibitory effect of Ser9 phosphorylation, up-regulates GSK-3β activity.
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