The rat β1 -subunit of the GABAA receptor forms a picrotoxin-sensitive anion channel open in the absence of GABA
- 6 November 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 257 (2) , 377-379
- https://doi.org/10.1016/0014-5793(89)81576-5
Abstract
The structural basis of GABA-gated chloride channels in mammalian brain is presently explored by the functonal expression of cDNAs coding for the α, β or γ-subunits of the receptor and their isoforms. In this context, we expressed the cloned cDNA coding for the rat β1-subunit of the GABAA receptor in the Xenopus oocyte. Surprisingly, efficient expression of a functional ion channel was found. The channel was anion-selective, and able to open in the absence of GABA. Since this channel could be shut by the GABA-channel blocker picrotoxin, we conclude that the β1 -subunit of the GABAA receptor is sufficient to form binding sites for picrotoxin.Keywords
This publication has 6 references indexed in Scilit:
- Importance of a novel GABAA receptor subunit for benzodiazepine pharmacologyNature, 1989
- Biophysical and pharmacological properties of cloned GABAA receptor subunits expressed in xenopus oocytesNeuron, 1988
- Single Subunits of the GABA A Receptor Form Ion Channels with Properties of the Native ReceptorScience, 1988
- Structural and functional basis for GABAA receptor heterogeneityNature, 1988
- Allosteric modulation by benzodiazepine receptor ligands of the GABAA receptor channel expressed in Xenopus oocytesJournal of Neuroscience, 1988
- Sequence and functional expression of the GABAA receptor shows a ligand-gated receptor super-familyNature, 1987