ArticleThe Journal of general physiology2008
Charge scan reveals an extended region at the intracellular end of the GABA receptor pore that can influence ion selectivity.
Article in The Journal of general physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- De novo variants in GABRA2 and GABRA5 alter receptor function and contribute to early-onset epilepsy.Brain : a journal of neurology · 2018Article
- Spillover transmission is mediated by the excitatory GABA receptor LGC-35 in C. elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Philosophy of voltage-gated proton channels.Journal of the Royal Society, Interface · 2014Review
- Mixed antagonistic effects of the ginkgolides at recombinant human ρ1 GABAC receptors.Neuropharmacology · 2012Article
- Discrete M3-M4 intracellular loop subdomains control specific aspects of γ-aminobutyric acid type A receptor function.The Journal of biological chemistry · 2011Article
- External divalent cations increase anion-cation permeability ratio in glycine receptor channels.Pflugers Archiv : European journal of physiology · 2010Article
- Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system.Nature reviews. Drug discovery · 2009Review
- Aplysia cys-loop glutamate-gated chloride channels reveal convergent evolution of ligand specificity.Journal of molecular evolution · 2009Article
- Anion-cation permeability correlates with hydrated counterion size in glycine receptor channels.Biophysical journal · 2008Article
- The cys-loop ligand-gated ion channel gene superfamily of the nematode, Caenorhabditis elegans.Invertebrate neuroscience : IN · 2008Article
Corrections and comments
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Authors and funding
2 authors.
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Abstract
Selective permeability is a fundamental property of ion channels. The Cys-loop receptor superfamily is composed of both excitatory (ACh, 5-HT) and inhibitory (GABA, glycine) neurotransmitter-operated ion channels. In the GABA receptor, it has been previously shown that the charge selectivity of the integral pore can be altered by a single mutation near the intracellular end of the second transmembrane-spanning domain (TM2). We have extended these findings and now show that charge selectivity of the anionic rho1 GABA receptor can be influenced by the introduction of glutamates, one at a time, over an 8-amino acid stretch (-2' to 5') in the proposed intracellular end of TM2 and the TM1-TM2 intracellular linker. Depending on the position, glutamate substitutions in this region produced sodium to chloride permeability ratios (P(Na)+(/Cl)-) varying from 0.64 to 3.4 (wild type P(Na)+(/Cl)- = 0). In addition to providing insight into the mechanism of ion selectivity, this functional evidence supports a model proposed for the homologous nicotinic acetylcholine receptor in which regions of the protein, in addition to TM2, form the ion pathway.
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