ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007
Na+/Cl- dipole couples agonist binding to kainate receptor activation.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Trapping of spermine, Kukoamine A, and polyamine toxin blockers in GluK2 kainate receptor channels.Nature communications · 2024Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Sex differences in the glutamate system: Implications for addiction.Neuroscience and biobehavioral reviews · 2020Review
- The structural arrangement at intersubunit interfaces in homomeric kainate receptors.Scientific reports · 2019Article
- Stargazin and cornichon-3 relieve polyamine block of AMPA receptors by enhancing blocker permeation.The Journal of general physiology · 2018Article
- Identification of critical functional determinants of kainate receptor modulation by auxiliary protein Neto2.The Journal of physiology · 2015Article
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- Retour aux sources: defining the structural basis of glutamate receptor activation.The Journal of physiology · 2015Review
- Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.Open biology · 2013Article
- Subunit-selective allosteric inhibition of glycine binding to NMDA receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Cations but not anions regulate the responsiveness of kainate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Ion-dependent gating of kainate receptors.The Journal of physiology · 2010Review
- A nondesensitizing kainate receptor point mutant.Molecular pharmacology · 2009Article
- Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.The EMBO journal · 2009Article
- Selectivity and cooperativity of modulatory ions in a neurotransmitter receptor.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kainate-selective ionotropic glutamate receptors (GluRs) require external Na+ and Cl- as well as the neurotransmitter L-glutamate for activation. Although, external anions and cations apparently coactivate kainate receptors (KARs) in an identical manner, it has yet to be established how ions of opposite charge achieve this. An additional complication is that KARs are subject to other forms of cation modulation via extracellular acidification (i.e., protons) and divalent ions. Consequently, other cation species may compete with Na+ to regulate the time KARs remain in the open state. Here we designed experiments to unravel how external ions regulate GluR6 KARs. We show that GluR6 kinetics are unaffected by alterations in physiological pH but that divalent and alkali metal ions compete to determine the time course of KAR channel activity. Additionally, Na+ and Cl- ions coactivate GluR6 receptors by establishing a dipole, accounting for their common effect on KARs. Using charged amino acids as tethered ions, we further demonstrate that the docking order is fixed with cations binding first, followed by anions. Together, our findings identify the dipole as a novel gating feature that couples neurotransmitter binding to KAR activation.
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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.