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Functional and molecular distinction between recombinant rat GABAA receptor subtypes by Zn2+

MPS-Authors
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Draguhn,  Andreas
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Ewert,  Markus
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Seeburg,  Peter H.
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Sakmann,  Bert
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Draguhn, A., Verdoorn, T. A., Ewert, M., Seeburg, P. H., & Sakmann, B. (1990). Functional and molecular distinction between recombinant rat GABAA receptor subtypes by Zn2+. Neuron, 5(6), 781-788. doi:10.1016/0896-6273(90)90337-F.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-AD34-3
Abstract
gamma-Aminobutyric acid receptor (GABAAR) channels in different neurons display heterogeneous functional properties. Molecular cloning revealed a large number of GABAAR subunits that assemble into GABAAR subtypes with different functional properties, suggesting that the subunit combination determines the functional properties of the receptor. In this study, the subunit composition of GABAARs is related to a functional distinction between Zn2(+)-sensitive and Zn2(+)-insensitive receptor subtypes. GABAARs reconstituted in transiently transfected fibroblasts from combinations of cDNAs encoding alpha and beta subunits are potently blocked by Zn2+. The presence of a gamma subunit in any combination with the other subunits leads to the formation of GABAARs that are almost insensitive to Zn2+. These data provide a structural correlate to the functional heterogeneity of the action of Zn2+ on GABAARs in native membranes and show that Zn2+ insensitivity of GABA-activated currents indicates the presence of a gamma-subunit in the assembled GABAAR channel.