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Journal Article

Stoichiometry of a recombinant GABAA receptor deduced from mutation-induced rectification

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Drescher,  U       
Department Physical Biology, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Backus, K., Arigoni, M., Drescher, U., Scheurer, L., Malherbe, P., Möhler, H., et al. (1993). Stoichiometry of a recombinant GABAA receptor deduced from mutation-induced rectification. NeuroReport, 5(3), 285-288. doi:10.1097/00001756-199312000-00026.


Cite as: https://hdl.handle.net/21.11116/0000-000D-F368-C
Abstract
Ligand-gated ion channels generally display a heterooligomeric subunit structure. The present report describes an electrophysiological method that provides criteria indicating the subunit stoichiometry of a recombinant GABAA receptor composed of alpha 3, beta 2 and gamma 2 subunits. Our results exclude the stoichiometries 3 alpha 1 beta 1 gamma, 1 alpha 3 beta 1 gamma, 1 alpha 1 beta 3 gamma and suggest that the possible subunit stoichiometries for this receptor are 2 alpha 1 beta 2 gamma, 2 alpha 2 beta 1 gamma or 1 alpha 2 beta 2 gamma, of which the alpha subunit composition 2 alpha 1 beta 2 gamma may be favoured. The method is based on the quantification of the outward rectification of the GABA-evoked current induced by point mutation of charged amino acids located near the ion channel pore.