Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism.

@article{Conricode1992ActivationOP,
  title={Activation of phospholipase D by protein kinase C. Evidence for a phosphorylation-independent mechanism.},
  author={K M Conricode and Kathryn A Brewer and John H. Exton},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 11},
  pages={7199-202}
}
The role of protein kinase C (PKC) in the regulation of phosphatidylcholine-hydrolyzing phospholipase D (PLD) was investigated. In membranes from Chinese hamster lung fibroblasts that had been incubated with [14C]choline to label endogenous phosphatidylcholine, phorbol 12-myristate 13-acetate (PMA) failed to stimulate production of [14C]choline. However, stimulation was observed if fibroblast cytosolic fraction or PKC partially purified from this fraction was added. When incubated with… CONTINUE READING