Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.

@article{Scheid2005PhosphoinositidedependentPO,
  title={Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.},
  author={Michael P. Scheid and Michael Parsons and James R Woodgett},
  journal={Molecular and cellular biology},
  year={2005},
  volume={25 6},
  pages={2347-63}
}
3-phosphoinositide-dependent kinase 1 (PDK1) phosphorylates the activation loop of a number of protein serine/threonine kinases of the AGC kinase superfamily, including protein kinase B (PKB; also called Akt), serum and glucocorticoid-induced kinase, protein kinase C isoforms, and the p70 ribosomal S6 kinase. PDK1 contains a carboxyl-terminal pleckstrin homology domain, which targets phosphoinositide lipids at the plasma membrane and is central to the activation of PKB. However, PDK1… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 30 extracted citations

Similar Papers

Loading similar papers…