Specific inhibition of the Akt1 pleckstrin homology domain by D-3-deoxy-phosphatidyl-myo-inositol analogues.

@article{Meuillet2003SpecificIO,
  title={Specific inhibition of the Akt1 pleckstrin homology domain by D-3-deoxy-phosphatidyl-myo-inositol analogues.},
  author={Emmanuelle J. Meuillet and Daruka Mahadevan and Hariprasad Vankayalapati and Margareta M. Berggren and Ryan D. Williams and Amy E Coon and Alan P. Kozikowski and Garth Powis},
  journal={Molecular cancer therapeutics},
  year={2003},
  volume={2 4},
  pages={389-99}
}
Activation of Akt (protein kinase B), a Ser/Thr protein kinase that promotes cell survival, has been linked to tumorigenesis. Akt is activated by phosphorylation after binding of its pleckstrin homology (PH) domain to plasma membrane phosphatidyl-myo-inositol-3-phosphates, formed by phosphoinositide-3-kinase. We report a novel strategy to inhibit Akt activation based on the use of D-3-deoxy-phosphatidyl-myo-inositols (DPIs) that cannot be phosphorylated on the 3-position of the myo-inositol… CONTINUE READING