ArticleThe Journal of general physiology2011
The long activations of α2 glycine channels can be described by a mechanism with reaction intermediates ("flip").
Article in The Journal of general physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Human GlyRα2 pore dynamics in gating and inhibition.Structure (London, England : 1993) · 2026Article
- Allosteric modulation and direct activation of glycine receptors by a tricyclic sulfonamide.Scientific reports · 2025Article
- The emerging role of glycine receptor α2 subunit defects in neurodevelopmental disorders.Frontiers in molecular neuroscience · 2025Review
- Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024Article
- Role of the Glycine Receptor β Subunit in Synaptic Localization and Pathogenicity in Severe Startle Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Loss, Gain and Altered Function of GlyR α2 Subunit Mutations in Neurodevelopmental Disorders.Frontiers in molecular neuroscience · 2022Article
- Modulatory Actions of the Glycine Receptor β Subunit on the Positive Allosteric Modulation of Ethanol in α2 Containing Receptors.Frontiers in molecular neuroscience · 2021Article
- Orthosteric and Allosteric Activation of Human 5-HTBiophysical journal · 2020Article
- Conformational dynamics and role of the acidic pocket in ASIC pH-dependent gating.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure-Function Analysis of the GlyR α2 Subunit Autism Mutation p.R323L Reveals a Gain-of-Function.Frontiers in molecular neuroscience · 2017Article
- In praise of single channel kinetics.The Journal of general physiology · 2016Article
- Altered development in GABA co-release shapes glycinergic synaptic currents in cultured spinal slices of the SOD1(G93A) mouse model of amyotrophic lateral sclerosis.The Journal of physiology · 2016Article
- Mechanism of activation of the prokaryotic channel ELIC by propylamine: a single-channel study.The Journal of general physiology · 2015Article
- Unraveling mechanisms underlying partial agonism in 5-HT3A receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Ionotropic GABA and glycine receptor subunit composition in human pluripotent stem cell-derived excitatory cortical neurones.The Journal of physiology · 2014Article
- GABAA receptor α and γ subunits shape synaptic currents via different mechanisms.The Journal of biological chemistry · 2014Article
- The kinetic properties of the α3 rat glycine receptor make it suitable for mediating fast synaptic inhibition.The Journal of physiology · 2013Article
- An outline of desensitization in pentameric ligand-gated ion channel receptors.Cellular and molecular life sciences : CMLS · 2013Review
- Perspectives on: conformational coupling in ion channels: allosteric coupling in ligand-gated ion channels.The Journal of general physiology · 2012Article
- The α1K276E startle disease mutation reveals multiple intermediate states in the gating of glycine receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
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5 authors.
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Abstract
The α2 glycine receptor (GlyR) subunit, abundant in embryonic neurons, is replaced by α1 in the adult nervous system. The single-channel activity of homomeric α2 channels differs from that of α1-containing GlyRs, as even at the lowest glycine concentration (20 µM), openings occurred in long (>300-ms) groups with high open probability (P(open); 0.96; cell-attached recordings, HEK-expressed channels). Shut-time intervals within groups of openings were dominated by short shuttings of 5-10 µs. The lack of concentration dependence in the groups of openings suggests that they represent single activations, separated by very long shut times at low concentrations. Several putative mechanisms were fitted by maximizing the likelihood of the entire sequence of open and shut times, with exact missed-events allowance (program hjcfit). Records obtained at several glycine concentrations were fitted simultaneously. The adequacy of the different schemes was judged by the accuracy with which they predicted not only single-channel data but also the time course and concentration dependence of macroscopic responses elicited by rapid glycine applications to outside-out patches. The data were adequately described only with schemes incorporating a reaction intermediate in the activation, and the best was a flip mechanism with two binding sites and one open state. Fits with this mechanism showed that for α2 channels, the opening rate constant is very fast, ∼130,000 s(-1), much as for α1β GlyRs (the receptor in mature synapses), but the estimated true mean open time is 20 times longer (around 3 ms). The efficacy for the flipping step and the binding affinity were lower for α2 than for α1β channels, but the overall efficacies were similar. As we previously showed for α1 homomeric receptors, in α2 glycine channels, maximum P(open) is achieved when fewer than all five of the putative binding sites in the pentamer are occupied by glycine.
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