S-Space College of Medicine/School of Medicine (의과대학/대학원) Dept. of Biochemistry & Molecular Biology (생화학교실) Journal Papers (저널논문_생화학교실)
Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells
- Kim, Yeni; Lee, Yun-Il; Seo, MiRan; Kim, So-Young; Youn, Hong-Duk; Juhnn, Yong-Sung; Kim, Yong-Sik; Lee, Ji-Eun
- Issue Date
- WILEY-BLACKWELL PUBLISHING, INC
- JOURNAL OF NEUROCHEMISTRY; Vol.111 2; 344-354
- This study examined the role of calcineurin, a major calcium-dependent protein phosphatase, in dephosphorylating Ser-9 and activating glycogen synthase kinase-3 beta (GSK-3 beta). Treatment with calcineurin inhibitors increased phosphorylation of GSK-3 beta at Ser-9 in SH-SY5Y human neuroblastoma cells. The over-expression of a constitutively active calcineurin mutant, calcineurin A beta (1-401), led to a significant decrease in phosphorylation at Ser-9, an increase in the activity of GSK-3 beta, and an increase in the phosphorylation of tau. K(m) of calcineurin for a GSK-3 beta phosphopeptide was 469.3 mu M, and specific activity of calcineurin was 15.2 nmol/min/mg. In addition, calcineurin and GSK-3 beta were co-immunoprecipitated in neuron-derived cells and brain tissues, and calcineurin formed a complex only with dephosphorylated GSK-3 beta. We conclude that in vitro, calcineurin can dephosphorylate GSK-3 beta at Ser-9 and form a stable complex with GSK-3 beta, suggesting the possibility that calcineurin regulates the dephosphorylation and activation of GSK-3 beta in vivo.
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