Carboxyl-terminal fragments of phospholipase C-beta1 with intrinsic Gq GTPase-activating protein (GAP) activity.

@article{Paulssen1996CarboxylterminalFO,
  title={Carboxyl-terminal fragments of phospholipase C-beta1 with intrinsic Gq GTPase-activating protein (GAP) activity.},
  author={Ruth H Paulssen and Jimmy Woodson and Songying Ouyang and Elliott M. Ross},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 43},
  pages={26622-9}
}
Fragments of the approximately 50 kDa COOH-terminal region of phospholipase C-beta1 (PLC-beta1(1)), ranging in size from 14 to 38 kDa, were expressed in Escherichia coli, purified, and tested for their regulatory activities. As expected, none of the fragments had phospholipase activity. Several fragments, referred to as PLC tails, displayed GTPase-activating protein (GAP) activity for Gq, the G protein class that stimulates the PLC-betas in response to receptors. Gq GAP activity is… CONTINUE READING