The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain.

@article{Brandizzi2002TheDF,
  title={The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain.},
  author={Federica Brandizzi and Nathalie Frangne and Sophie Marc-Martin and Chris Hawes and J. -M. Neuhaus and Nadine Paris},
  journal={The Plant cell},
  year={2002},
  volume={14 5},
  pages={1077-92}
}
The tonoplast was proposed as a default destination of membrane-bound proteins without specific targeting signals. To investigate the nature of this targeting, we created type I fusion proteins with green fluorescent protein followed by the transmembrane domain of the human lysosomal protein LAMP1. We varied the length of the transmembrane domain from 23 to either 20 or 17 amino acids by deletion within the hydrophobic domain. The resulting chimeras, called TM23, TM20, and TM17, were expressed… CONTINUE READING
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