ArticleThe Journal of biological chemistry2016
Toward Understanding Functional Properties and Subunit Arrangement of α4β2δ γ-Aminobutyric Acid, Type A (GABAA) Receptors.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Molecular arrangement and modulation of extrasynaptic αβδ GABANature communications · 2026Article
- The human GABAbioRxiv : the preprint server for biology · 2026Article
- The human GABAmicroPublication biology · 2026Article
- Decoding the structural and functional diversity of GABAFrontiers in pharmacology · 2025Review
- Navigating the complex landscape of benzodiazepine- and Z-drug diversity: insights from comprehensive FDA adverse event reporting system analysis and beyond.Frontiers in psychiatry · 2023Article
- Structural determinants and regulation of spontaneous activity in GABANature communications · 2021Article
- Pharmacological and Biophysical Characteristics of Picrotoxin-Resistant, δSubunit-Containing GABAFrontiers in synaptic neuroscience · 2021Article
- Allosteric GABAMolecules (Basel, Switzerland) · 2020Review
- Binding site location on GABABritish journal of pharmacology · 2019Article
- Steady-state activation of the high-affinity isoform of the α4β2δ GABAScientific reports · 2019Article
- Comparison of αβδ and αβγ GABAPharmacological research · 2018Review
- Administration of AlphaBiomolecules & therapeutics · 2018Article
- Article
- Assembly rules for GABAeLife · 2017Article
- Article
- Xenopus Oocytes: Optimized Methods for Microinjection, Removal of Follicular Cell Layers, and Fast Solution Changes in Electrophysiological Experiments.Journal of visualized experiments : JoVE · 2016Article
- General Anesthetic Binding Sites in Human α4β3δ γ-Aminobutyric Acid Type A Receptors (GABAARs).The Journal of biological chemistry · 2016Article
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Authors and funding
3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
GABAA receptors are pentameric ligand-gated channels mediating inhibitory neurotransmission in the CNS. α4βxδ GABAA receptors are extrasynaptic receptors important for tonic inhibition. The functional properties and subunit arrangement of these receptors are controversial. We predefined subunit arrangement by using subunit concatenation. α4, β2, and δ subunits were concatenated to dimeric, trimeric, and, in some cases, pentameric subunits. We constructed in total nine different receptor pentamers in at least two different ways and expressed them in Xenopus oocytes. The δ subunit was substituted in any of the five positions in the α1β2 receptor. In addition, we investigated all receptors with the 2:2:1 subunit stoichiometry for α4, β2, and δ. Several functional receptors were obtained. Interestingly, all of these receptors had very similar EC50 values for GABA in the presence of the neurosteroid 3α, 21-dihydroxy-5α-pregnan-20-one (THDOC). All functional receptors containing δ subunits were sensitive to 4-chloro-N-[2-(2-thienyl)imidazo[1,2-a]pyridin-3-yl]benzamide (DS2). Moreover, none of the receptors was affected by ethanol up to 30 mm These properties recapitulate those of non-concatenated receptors expressed from a cRNA ratio of 1:1:5 coding for α4, β2, and δ subunits. We conclude that the subunit arrangement of α4β2δ GABAA receptors is not strongly predefined but is mostly satisfying the 2:2:1 subunit stoichiometry for α4, β2, and δ subunits and that several subunit arrangements result in receptors with similar functional properties tuned to physiological conditions.
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