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ABSTRACT: Rationale
GSK-3β (glycogen synthase kinase 3β) is a multifunctional and constitutively active kinase known to regulate a myriad of cellular processes. The primary mechanism to regulate its function is through phosphorylation-dependent inhibition at serine-9 residue. Emerging evidence indicates that there may be alternative mechanisms that control GSK-3β for certain functions.Objectives
Here, we sought to understand the role of protein S-nitrosylation (SNO) on the function of GSK-3β. SNO-dependent modulation of the localization of GSK-3β and its ability to phosphorylate downstream targets was investigated in vitro, and the network of proteins differentially impacted by phospho- or SNO-dependent GSK-3β regulation and in vivo SNO modification of key signaling kinases du
SUBMITTER: Wang SB
PROVIDER: S-EPMC6047766 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature