Glycosylation of a vesicular monoamine transporter: a mutation in a conserved proline residue affects the activity, glycosylation, and localization of the transporter.

@article{Yelin1998GlycosylationOA,
  title={Glycosylation of a vesicular monoamine transporter: a mutation in a conserved proline residue affects the activity, glycosylation, and localization of the transporter.},
  author={Rodrigo Yelin and Sonia Steiner-Mordoch and Benjamin Aroeti and Shimon Schuldiner},
  journal={Journal of neurochemistry},
  year={1998},
  volume={71 6},
  pages={2518-27}
}
The role of N-glycosylation in the expression, ligand recognition, activity, and intracellular localization of a rat vesicular monoamine transporter (rVMAT1) was investigated. The glycosylation inhibitor tunicamycin induced a dose-dependent decrease in the rVMAT1-mediated uptake of [3H]serotonin. Part of this effect was due to a general toxic effect of the drug. Therefore, to assess the contribution of each of the glycosylation sites to the transporter activity, the three putative N… CONTINUE READING
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