Gbetagamma and palmitate target newly synthesized Galphaz to the plasma membrane.

@article{Fishburn1999GbetagammaAP,
  title={Gbetagamma and palmitate target newly synthesized Galphaz to the plasma membrane.},
  author={C. Simone Fishburn and Paul Herzmark and Janine M. Morales and Henry R. Bourne},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 26},
  pages={18793-800}
}
The subcellular location of a signaling protein determines its ability to transmit messages accurately and efficiently. Three different lipid modifications tether heterotrimeric G proteins to membranes: alpha subunits are myristoylated and/or palmitoylated, and gamma subunits are prenylated. In a previous study, we examined the role of lipid modifications in maintaining the membrane attachment of a G protein alpha subunit, alphaz, which is myristoylated and palmitoylated (Morales, J., Fishburn… CONTINUE READING

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