Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A.

@article{Fang2000PhosphorylationAI,
  title={Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A.},
  author={Xianjun Fang and Shuang Yu and Yiling Lu and Robert C. Bast and James R Woodgett and Gordon B. Mills},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 22},
  pages={11960-5}
}
Glycogen synthase kinase 3 (GSK-3) is implicated in multiple biological processes including metabolism, gene expression, cell fate determination, proliferation, and survival. GSK-3 activity is inhibited through phosphorylation of serine 21 in GSK-3 alpha and serine 9 in GSK-3 beta. These serine residues of GSK-3 have been previously identified as targets of protein kinase B (PKB/Akt), a serine/threonine kinase located downstream of phosphatidylinositol 3-kinase. Here, we show that serine 21 in… CONTINUE READING
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Development (Cambridge, U.K

  • S. E. Plyte, E. O’Donovan, J. R. Woodgett, J HarwoodA.
  • 1999

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