Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis

@article{Peters1992PointMO,
  title={Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis},
  author={Kevin G. Peters and Jacky Marie and Emily M F Wilson and Harlan E. Ives and Jaime Escobedo and Mercedita Del Rosario and Daniel Mirda and Lewis T. Williams},
  journal={Nature},
  year={1992},
  volume={358},
  pages={678-681}
}
STIMULATION of certain receptor tyrosine kinases results in the tyrosine phosphorylation and activation of phospholipase Cγ(PLCγ), an enzyme that catalyses the hydrolysis of phosphatidylinositol (Ptdlns)1–8. This hydrolysis generates diacylglycerol and free inositol phosphate, which in turn activate protein kinase C and increase intracellular Ca2+, respectively. PLCγ physically associates with activated receptor tyrosine kinases, suggesting that it is a substrate for direct phosphorylation by… CONTINUE READING