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Updated: Aug 8, 2026

Single Cell Measurement of Dopamine Release with Simultaneous Voltage-clamp and Amperometry
Published on: November 21, 2012
Zn(2+) site engineering at the oligomeric interface of the dopamine transporter
Kristine Norgaard-Nielsen1, Lene Norregaard, Hanne Hastrup
1Molecular Neuropharmacology Group, Department of Pharmacology 12-5-22, The Panum Institute, University of Copenhagen, DK-2200 N Copenhagen, Denmark.
Abstract:
Increasing evidence suggests that Na(+)/Cl(-)-dependent neurotransmitter transporters exist as homo-oligomeric proteins. However, the functional implication of this oligomerization remains unclear. Here we demonstrate the engineering of a Zn(2+) binding site at the predicted dimeric interface of the dopamine transporter (DAT) corresponding to the external end of transmembrane segment 6. Upon binding to this site, which involves a histidine inserted in position 310 (V310H) and the endogenous Cys306 within the same DAT molecule, Zn(2+) potently inhibits [(3)H]dopamine uptake. These data provide indirect evidence that conformational changes critical for the translocation process may occur at the interface between two transporter molecules in the oligomeric structure.
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