E-mail a Wiley Online Library Link

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

Version of Record online: 30 MAY 2013 | DOI: 10.1111/jnc.12285

Thumbnail image of graphical abstract

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.

Complete the form below and we will send an e-mail message containing a link to the selected article on your behalf

Required = Required Field