GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.

@article{Vries1996GAIPIM,
  title={GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.},
  author={l Jolanda M de Vries and Eric Elenko and L Hubler and Teresa L. Z. Jones and Marilyn Gist Farquhar},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1996},
  volume={93 26},
  pages={15203-8}
}
GAIP (G Alpha Interacting Protein) is a member of the recently described RGS (Regulators of G-protein Signaling) family that was isolated by interaction cloning with the heterotrimeric G-protein G alpha i3 and was recently shown to be a GTPase-activating protein (GAP). In AtT-20 cells stably expressing GAIP, we found that GAIP is membrane-anchored and faces the cytoplasm, because it was not released by sodium carbonate treatment but was digested by proteinase K. When Cos cells were transiently… CONTINUE READING
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