ArticleProceedings of the National Academy of Sciences of the United States of America2009
Energetics of glutamate receptor ligand binding domain dimer assembly are modulated by allosteric ions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 49 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
- Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural biology and thermodynamics of GluD receptors.Neuropharmacology · 2021Review
- Cryo-EM structures of the ionotropic glutamate receptor GluD1 reveal a non-swapped architecture.Nature structural & molecular biology · 2020Article
- The structure and function of glutamate receptors: MgNeuropharmacology · 2017Review
- Article
- Article
- Identification of critical functional determinants of kainate receptor modulation by auxiliary protein Neto2.The Journal of physiology · 2015Article
- Glycine activated ion channel subunits encoded by ctenophore glutamate receptor genes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Intracellular Cl- as a signaling ion that potently regulates Na+/HCO3- transporters.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- Calcium affects OX1 orexin (hypocretin) receptor responses by modifying both orexin binding and the signal transduction machinery.British journal of pharmacology · 2014Article
- Intersubunit conformational changes mediate epithelial sodium channel gating.The Journal of general physiology · 2014Article
- The N-terminal domain modulates α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor desensitization.The Journal of biological chemistry · 2014Article
- A hard-wired glutamatergic circuit pools and relays UV signals to mediate spectral preference in Drosophila.Neuron · 2014Article
- Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.Open biology · 2013Article
- Anions mediate ligand binding in Adineta vaga glutamate receptor ion channels.Structure (London, England : 1993) · 2013Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The activity of many ligand-gated ion channels and cell surface receptors is modulated by small molecules and ions, but an understanding of the underlying molecular mechanisms is scarce. For kainate, but not AMPA subtype glutamate receptors, the binding of Na(+) and Cl(-) ions to discrete, electrostatically coupled sites in the extracellular ligand binding domain (LBD) dimer assembly regulates the rate of entry into the desensitized state, which occurs when the dimer interface ruptures and the channel closes. Studies on glutamate receptors have defined the LBD dimer assembly as a key functional unit that controls activation and desensitization. Here we use analytical ultracentrifugation to probe the energetic effects of allosteric ions on kainate receptor dimer stability in solution, using a GluR6 mutant that desensitizes slowly. Our results show that sodium and chloride ions modulate kainate receptor dimer affinity as much as 50-fold, and that removal of either Cl(-) or Na(+) disrupts the dimer. The applicability of a similar allosteric mechanism for modulation of delta2 glutamate receptors by Ca(2+) was also tested. Our results indicate that ions can contribute substantial free energy to active state stabilization in both these receptors, and provide quantitative measurements of the energetic consequences of allosteric ion binding to a ligand-gated ion channel.
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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.