The Role of Zinc Ions in Reverse Transport Mediated by Monoamine Transporters*

@article{Scholze2002TheRO,
  title={The Role of Zinc Ions in Reverse Transport Mediated by Monoamine Transporters*},
  author={P. Scholze and L. Norregaard and E. Singer and M. Freissmuth and U. Gether and H. Sitte},
  journal={The Journal of Biological Chemistry},
  year={2002},
  volume={277},
  pages={21505 - 21513}
}
  • P. Scholze, L. Norregaard, +3 authors H. Sitte
  • Published 2002
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
    • The human dopamine transporter (hDAT) contains an endogenous high affinity Zn2+ binding site with three coordinating residues on its extracellular face (His193, His375, and Glu396). Upon binding to this site, Zn2+ causes inhibition of [3H]1-methyl-4-phenylpyridinium ([3H]MPP+) uptake. We investigated the effect of Zn2+ on outward transport by superfusing hDAT-expressing HEK-293 cells preloaded with [3H]MPP+. Although Zn2+ inhibited uptake, Zn2+facilitated [3H]MPP+ release induced by amphetamine… CONTINUE READING
    View on ASBMB
    jbc.org
    89 Citations
    Highly Influential Citations
    6
    Background Citations
    43
    Methods Citations
    6
    Results Citations
    2
    89 Citations
    Citation Type

    Citation Type

    Aspartate 345 of the Dopamine Transporter Is Critical for Conformational Changes in Substrate Translocation and Cocaine Binding*
    • 46
    • PDF
    Occupancy of the Zinc-binding Site by Transition Metals Decreases the Substrate Affinity of the Human Dopamine Transporter by an Allosteric Mechanism*
    • 16
    • PDF
    Zinc regulates the dopamine transporter in a membrane potential and chloride dependent manner
    • 30
    • PDF
    Dual Action of Zn2+ on the Transport Cycle of the Dopamine Transporter*
    • 22
    • PDF
    Insights From Endogenous and Engineered Zn2+ Binding Sites in Monoamine Transporters
    Zn2+ modulates currents generated by the dopamine transporter: parallel effects on amphetamine-induced charge transfer and release
    • 23
    • PDF
    Zinc Potentiates an Uncoupled Anion Conductance Associated with the Dopamine Transporter*
    • 52
    • PDF
    Probing dopamine transporter structure and function by Zn2+-site engineering.
    • 37
    Zn2+ modulation of neurotransmitter transporters.
    • 22
    A Juxtamembrane Mutation in the N Terminus of the Dopamine Transporter Induces Preference for an Inward-Facing Conformation
    • 65
    • Highly Influenced
    • PDF

    References

    SHOWING 1-10 OF 44 REFERENCES
    Delineation of an endogenous zinc‐binding site in the human dopamine transporter
    • 181
    • PDF
    Molecular basis for differential inhibition of glutamate transporter subtypes by zinc ions.
    • 101
    • PDF
    Engineered Zn(2+) switches in the gamma-aminobutyric acid (GABA) transporter-1. Differential effects on GABA uptake and currents.
    • 38
    Defining Proximity Relationships in the Tertiary Structure of the Dopamine Transporter
    • 103
    • PDF
    Structural probing of a microdomain in the dopamine transporter by engineering of artificial Zn2+ binding sites.
    • 36
    Ion dependence of carrier-mediated release in dopamine or norepinephrine transporter-transfected cells questions the hypothesis of facilitated exchange diffusion.
    • 58
    • PDF
    Quantitative analysis of inward and outward transport rates in cells stably expressing the cloned human serotonin transporter: inconsistencies with the hypothesis of facilitated exchange diffusion.
    • 64
    • PDF
    Zinc modulation of drug binding, cocaine affinity states, and dopamine uptake on the dopamine uptake complex.
    • 56
    Micromolar concentrations of Zn2+ antagonize NMDA and GABA responses of hippocampal neurons
    • 816
    Chimeric dopamine-norepinephrine transporters delineate structural domains influencing selectivity for catecholamines and 1-methyl-4-phenylpyridinium.
    • K. Buck, S. Amara
    • Biology, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 1994
    • 234
    • PDF