ArticleThe Journal of physiology2005
Molecular determinants of glycine receptor alphabeta subunit sensitivities to Zn2+-mediated inhibition.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 54 citations in OpenAlex.
- Molecular correlates of glycine receptor activity in human β cells.Molecular metabolism · 2025Article
- Mechanisms underlying modulation of human GlyRα3 by ZnScience advances · 2024Article
- A System for Assessing Dual Action Modulators of Glycine Transporters and Glycine Receptors.Biomolecules · 2020Article
- Zinc as a Neuromodulator in the Central Nervous System with a Focus on the Olfactory Bulb.Frontiers in cellular neuroscience · 2017Review
- Structure and Pharmacologic Modulation of Inhibitory Glycine Receptors.Molecular pharmacology · 2016Review
- Murine startle mutant Nmf11 affects the structural stability of the glycine receptor and increases deactivation.The Journal of physiology · 2016Article
- The Free Zinc Concentration in the Synaptic Cleft of Artificial Glycinergic Synapses Rises to At least 1 μM.Frontiers in molecular neuroscience · 2016Article
- Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses.Pharmacological research · 2015Review
- Allosteric modulation of the glycine receptor activated by agonists differing in efficacy.Brain research · 2015Article
- Zinc-dependent modulation of α2- and α3-glycine receptor subunits by ethanol.Alcoholism, clinical and experimental research · 2013Article
- The Concise Guide to PHARMACOLOGY 2013/14: ligand-gated ion channels.British journal of pharmacology · 2013Article
- The GLRA1 missense mutation W170S associates lack of Zn2+ potentiation with human hyperekplexia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Mutation of a zinc-binding residue in the glycine receptor α1 subunit changes ethanol sensitivity in vitro and alcohol consumption in vivo.The Journal of pharmacology and experimental therapeutics · 2013Article
- Synaptic neurotransmitter-gated receptors.Cold Spring Harbor perspectives in biology · 2012Review
- Article
- Fast synaptic inhibition in spinal sensory processing and pain control.Physiological reviews · 2012Review
- Allosteric modulation of glycine receptors.British journal of pharmacology · 2011Review
- Zinc modulation of glycine receptors.Neuroscience · 2011Article
- Pulsed electron spin resonance resolves the coordination site of Cu²(+) ions in α1-glycine receptor.Biophysical journal · 2010Article
- Zinc enhances ethanol modulation of the alpha1 glycine receptor.Neuropharmacology · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Glycine receptors exhibit a biphasic sensitivity profile in response to Zn2+-mediated modulation, with low Zn2+ concentrations potentiating (< 10 microm), and higher Zn2+ concentrations inhibiting submaximal responses to glycine. Here, a substantial 30-fold increase in sensitivity to Zn2+-mediated inhibition was apparent for the homomeric glycine receptor (GlyR) alpha1 subunit compared to either GlyR alpha2 or alpha3 subtypes. Swapping the divergent histidine (H107) residue in GlyR alpha1, which together with the conserved H109 forms part of an intersubunit Zn2+-binding site, for the equivalent asparagine residue present in GlyR alpha2 and alpha3, reversed this phenotype. Co-expression of heteromeric GlyR alpha1 or alpha2 with the ancillary beta subunit yielded receptors that maintained their distinctive sensitivities to Zn2+ inhibition. However, GlyR alpha2beta heteromers were consistently 2-fold more sensitive to inhibition compared to the GlyR alpha2 homomer. Comparative studies to elucidate the specific residue in the beta subunit responsible for this differential sensitivity revealed instead threonine 133 in the alpha1 subunit as a new vital component for Zn2+-mediated inhibition. Further studies on heteromeric receptors demonstrated that a mutated beta subunit could indeed affect Zn2+-mediated inhibition but only from one side of the intersubunit Zn2+-binding site, equivalent to the GlyR alpha1 H107 face. This strongly suggests that the alpha subunit is responsible for Zn2+-mediated inhibition and that this is effectively transduced, asymmetrically, from the side of the Zn2+-binding site where H109 and T133 are located.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.