ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
Conformational flexibility of the ligand-binding domain dimer in kainate receptor gating and desensitization.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 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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20 citing papers in PubMed, 30 citations in OpenAlex.
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Mechanism of partial agonism in AMPA-type glutamate receptors.Nature communications · 2017Article
- Distinct Structural Pathways Coordinate the Activation of AMPA Receptor-Auxiliary Subunit Complexes.Neuron · 2016Article
- Molecular Dynamics Investigation of gluazo, a Photo-Switchable Ligand for the Glutamate Receptor GluK2.PloS one · 2015Article
- Ionotropic glutamate receptors: alive and kicking.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
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
- Modulation of homomeric and heteromeric kainate receptors by the auxiliary subunit Neto1.The Journal of physiology · 2013Article
- Defining the structural relationship between kainate-receptor deactivation and desensitization.Nature structural & molecular biology · 2013Article
- Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.Open biology · 2013Article
- Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functional insights from glutamate receptor ion channel structures.Annual review of physiology · 2013Review
- GIRAF: a method for fast search and flexible alignment of ligand binding interfaces in proteins at atomic resolution.Biophysics (Nagoya-shi, Japan) · 2012Article
- Not all desensitizations are created equal: physiological evidence that AMPA receptor desensitization differs for kainate and glutamate.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
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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
AMPA- and kainate (KA)-selective ionotropic glutamate receptors (iGluRs) respond to agonist by opening (gating), then closing (desensitizing) in quick succession. Gating has been linked to agonist-induced changes within the ligand-binding domain (LBD), and desensitization to rearrangement of a dimer formed by neighboring LBDs. To explore the role of dimer conformation in both gating and desensitization, we compared the conformational effects of two kainate receptor mutants. The first, GluK2-D776K, blocks desensitization of macroscopic current responses ("macroscopic desensitization"). The second, GluK2-M770K, accelerates macroscopic desensitization and eliminates the effects of external ions on channel kinetics. Using structures determined by x-ray crystallography, we found that in both mutants the introduced lysines act as tethered cations, displacing sodium ions from their binding sites within the dimer interface. This results in new inter- and intra-protomer contacts in D776K and M770K respectively, explaining the effects of these mutations on dimer stability and desensitization kinetics. Further, chloride binding was unaffected by the M770K mutation, even though binding of sodium ions has been proposed to promote dimer stability by stabilizing anion binding. This suggests sodium binding may affect receptor function more directly than currently supposed. Notably, we also observed a ligand-specific shift in dimer conformation when comparing LBD dimers in complex with glutamate or the partial agonist KA, revealing a previously unidentified role for dimer orientation in iGluR gating.
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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.