Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells.

@article{Kim2009CalcineurinDG,
  title={Calcineurin dephosphorylates glycogen synthase kinase-3 beta at serine-9 in neuroblast-derived cells.},
  author={Yeni Kim and Yun-il Lee and Miran Seo and So-young Kim and Ji-Eun Lee and Hong-Duk Youn and Yong-Sik Kim and Y. -S. Juhnn},
  journal={Journal of neurochemistry},
  year={2009},
  volume={111 2},
  pages={344-54}
}
This study examined the role of calcineurin, a major calcium-dependent protein phosphatase, in dephosphorylating Ser-9 and activating glycogen synthase kinase-3beta (GSK-3beta). Treatment with calcineurin inhibitors increased phosphorylation of GSK-3beta 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-3beta… CONTINUE READING

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