Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus.

@article{Feldman2002SelectiveIO,
  title={Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus.},
  author={David S. Feldman and Alberuni Musa Zamah and Kristen L. Pierce and William E Miller and Francine Kelly and Antonio Rapacciuolo and Howard A Rockman and Walter J Koch and Louis M Luttrell},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 32},
  pages={28631-40}
}
The blockade of heptahelical receptor coupling to heterotrimeric G proteins by the expression of peptides derived from G protein Galpha subunits represents a novel means of simultaneously inhibiting signals arising from multiple receptors that share a common G protein pool. Here we examined the mechanism of action and functional consequences of expression of an 83-amino acid polypeptide derived from the carboxyl terminus of Galpha(s) (GsCT). In membranes prepared from GsCT-expressing cells, the… CONTINUE READING

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