We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells.
- Authors
Yeni Kim; Yun-Il Lee; Seo, MiRan; So-Young Kim; Ji-Eun Lee; Hong-Duk Youn; Yong-Sik Kim; Yong-Sung Juhnn
- Abstract
This study examined the role of calcineurin, a major calcium-dependent protein phosphatase, in dephosphorylating Ser-9 and activating glycogen synthase kinase-3β (GSK-3β). Treatment with calcineurin inhibitors increased phosphorylation of GSK-3β 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-3β, and an increase in the phosphorylation of tau. Km of calcineurin for a GSK-3β phosphopeptide was 469.3 μM, and specific activity of calcineurin was 15.2 nmol/min/mg. In addition, calcineurin and GSK-3β were co-immunoprecipitated in neuron-derived cells and brain tissues, and calcineurin formed a complex only with dephosphorylated GSK-3β. We conclude that in vitro, calcineurin can dephosphorylate GSK-3β at Ser-9 and form a stable complex with GSK-3β, suggesting the possibility that calcineurin regulates the dephosphorylation and activation of GSK-3β in vivo.
- Subjects
PHOSPHORYLATION; GLUCANS; NEUROBLASTOMA; GLYCOGEN synthesis; GLYCOGEN synthase kinase-3
- Publication
Journal of Neurochemistry, 2009, Vol 111, Issue 2, p344
- ISSN
0022-3042
- Publication type
Article
- DOI
10.1111/j.1471-4159.2009.06318.x