Role of the Phox homology domain and phosphorylation in activation of serum and glucocorticoid-regulated kinase-3.

@article{Tessier2006RoleOT,
  title={Role of the Phox homology domain and phosphorylation in activation of serum and glucocorticoid-regulated kinase-3.},
  author={Maude Tessier and James R Woodgett},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 33},
  pages={23978-89}
}
Serum and glucocorticoid-regulated kinases (SGKs) form a family of serine/threonine protein kinases that exhibit structural and sequence similarity to the protein kinase B (PKB)/Akt family. The major difference between these two families is the absence of a lipid-binding, pleckstrin homology domain in the SGKs. Despite the absence of the pleckstrin homology domain, activation of the three human isoforms is, like PKB, dependent upon the phosphatidylinositol 3'-kinase (PI3K) pathway that is… CONTINUE READING

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