Transmembrane domain III plays an important role in ion binding and permeation in the glycine transporter GLYT2.

@article{Ponce2000TransmembraneDI,
  title={Transmembrane domain III plays an important role in ion binding and permeation in the glycine transporter GLYT2.},
  author={Jos{\'e} Vicente Gil Ponce and Bruno Biton and J{\'e}sus Benavides and Patrick Avenet and Carmen Arag{\'o}n},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 18},
  pages={13856-62}
}
The neuronal glycine transporter GLYT2 takes up glycine from the extracellular space by an electrogenic process where this neurotransmitter is co-transported with sodium and chloride ions. We report in this paper that tyrosine at position 289 of GLYT2a is crucial for ion coupling, glycine affinity and sodium selectivity, stressing the essential role played by this residue of transmembrane domain III in the mechanism of transport. Substitution to tryptophan (Y289W), phenylalanine (Y289F), or… CONTINUE READING