PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells

@article{Auger1989PDGFdependentTP,
  title={PDGF-dependent tyrosine phosphorylation stimulates production of novel polyphosphoinositides in intact cells},
  author={Kurt R. Auger and Leslie A. Serunian and Stephen P. Soltoff and Peter Libby and Lewis C. Cantley},
  journal={Cell},
  year={1989},
  volume={57},
  pages={167-175}
}
A phosphatidylinositol (PI) kinase activity associated with certain protein tyrosine kinases important in cell proliferation phosphorylates the 3' hydroxyl position of PI to produce phosphatidylinositol-3-phosphate (PI-3-P). Here we report that, in addition to PI-3' kinase activity, anti-phosphotyrosine (alpha-P-tyr) immunoprecipitates from platelet-derived growth factor (PDGF)-stimulated smooth muscle cells (SMC) contain lipid kinase activities that utilize the substrates phosphatidylinositol… Expand
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  • Biology, Medicine
  • Biochemical and biophysical research communications
  • 1990
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TLDR
Experiments using sodium periodate and selective phosphatase enzymes to degrade this compound systematically generated a series of products which suggested the structure of the parent phospholipid was phosphatidyl-myo-inositol 3-phosphate (PtdIns3P), which suggests that all three polyphosphoinositides are synthesized from a common, rapidly metabolized, pool of phosphatids. Expand
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