Palmitoylation of human endothelinB. Its critical role in G protein coupling and a differential requirement for the cytoplasmic tail by G protein subtypes.

@article{Okamoto1997PalmitoylationOH,
  title={Palmitoylation of human endothelinB. Its critical role in G protein coupling and a differential requirement for the cytoplasmic tail by G protein subtypes.},
  author={Yukihiro Okamoto and Haruaki Ninomiya and Maki Tanioka and Ayako Sakamoto and Soichi Miwa and Tomoh Masaki},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 34},
  pages={21589-96}
}
By site-directed mutagenesis, three cysteine residues (amino acids 402, 403, and 405) in the carboxyl terminus of human endothelinB (ETB) were identified as potential palmitoylation sites. Substitutions of all of the three cysteine residues with serine gave an unpalmitoylated mutant, C2S/C3S/C5S. When expressed in Chinese hamster ovary cells, C2S/C3S/C5S was localized on the cell surface, retained high affinities to ET-1 and ET-3, and was rapidly internalized when bound to the ligand. However… CONTINUE READING

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