ArticleThe EMBO journal2009
Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.
Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 54 citations in OpenAlex.
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Multilayer control of KaiR1D-autoreceptor function by the auxiliary protein Neto.bioRxiv : the preprint server for biology · 2025Article
- Structure and gating of kainate receptors.Frontiers in pharmacology · 2025Review
- Rice-produced classical swine fever virus glycoprotein E2 with herringbone-dimer design to enhance immune responses.Plant biotechnology journal · 2023Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Universal Architectural Concepts Underlying Protein Folding Patterns.Frontiers in molecular biosciences · 2020Article
- Competition between LiChemical science · 2018Article
- Functional Validation of Heteromeric Kainate Receptor Models.Biophysical journal · 2017Article
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- Protons Potentiate GluN1/GluN3A Currents by Attenuating Their Desensitisation.Scientific reports · 2016Article
- Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter.PLoS biology · 2016Article
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Acta crystallographica. Section D, Biological crystallography · 2015Article
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- Contributions of different kainate receptor subunits to the properties of recombinant homomeric and heteromeric receptors.Neuroscience · 2014Article
- Tethered ligands reveal glutamate receptor desensitization depends on subunit occupancy.Nature chemical biology · 2014Article
- 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
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
AMPA and kainate receptors mediate fast synaptic transmission. AMPA receptor ligand-binding domains form dimers, which are key functional units controlling ion-channel activation and desensitization. Dimer stability is inversely related to the rate and extent of desensitization. Kainate and AMPA receptors share common structural elements, but functional measurements suggest that subunit assembly and gating differs between these subtypes. To investigate this, we constructed a library of GluR6 kainate receptor mutants and directly measured changes in kainate receptor dimer stability by analytical ultracentrifugation, which, combined with electrophysiological experiments, revealed an inverse correlation between dimer stability and the rate of desensitization. We solved crystal structures for a series of five GluR6 mutants, to understand the molecular mechanisms for dimer stabilization. We demonstrate that the desensitized state of kainate receptors acts as a deep energy well offsetting the stabilizing effects of dimer interface mutants, and that the deactivation of kainate receptor responses is dominated by entry into desensitized states. Our results show how neurotransmitter receptors with similar structures and gating mechanisms can exhibit strikingly different functional properties.
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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.