Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity.

@article{Singer1996RegulationOP,
  title={Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity.},
  author={William D. Singer and Haley A Brown and Xuejun Jiang and Paul C. Sternweis},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 8},
  pages={4504-10}
}
Phospholipase D (PLD) which was partially purified from membranes of porcine brain could be stimulated by multiple cytosolic components; these included ADP-ribosylation factor (Arf) and RhoA, which required guanine nucleotides for activity, and an unidentified factor which activated the enzyme in a nucleotide-independent manner (Singer, W. D., Brown, H. A., Bokoch, G. M., and Sternweis, P. C. (1995) J. Biol. Chem. 270, 14944-14950). Here, we report purification of the latter factor, its… CONTINUE READING

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