ArticleThe Journal of physiology2013
Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state.
Article in The Journal of physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Tuning of AMPA receptor activation by inhibitory auxiliary subunits and epilepsy-associated disease mutations.Nature communications · 2026Article
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- Structural insights into kainate receptor desensitization.Nature communications · 2025Article
- The gating properties of Drosophila NMJ glutamate receptors and their dependence on Neto.The Journal of physiology · 2024Article
- Neto proteins differentially modulate the gating properties ofbioRxiv : the preprint server for biology · 2024Article
- Loss of activation by GABA in vertebrate delta ionotropic glutamate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The action of Con-ikot-ikot toxin on single AMPA-type glutamate receptors.The Journal of general physiology · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Mutation of a conserved glutamine residue does not abolish desensitization of acid-sensing ion channel 1.The Journal of general physiology · 2021Article
- Molecular Investigation of Chicken Acid-Sensing Ion Channel 1 β11-12 Linker Isomerization and Channel Kinetics.Frontiers in cellular neuroscience · 2021Article
- Article
- Polyamine-mediated channel block of ionotropic glutamate receptors and its regulation by auxiliary proteins.The Journal of biological chemistry · 2018Review
- Shared and unique aspects of ligand- and voltage-gated ion-channel gating.The Journal of physiology · 2018Article
- Unitary Properties of AMPA Receptors with Reduced Desensitization.Biophysical journal · 2017Article
- Pharmacology and Structural Analysis of Ligand Binding to the Orthosteric Site of Glutamate-Like GluD2 Receptors.Molecular pharmacology · 2016Article
- Probing Intersubunit Interfaces in AMPA-subtype Ionotropic Glutamate Receptors.Scientific reports · 2016Article
- Ionotropic glutamate receptors: alive and kicking.The Journal of physiology · 2015Article
- Retour aux sources: defining the structural basis of glutamate receptor activation.The Journal of physiology · 2015Review
- The multifaceted subunit interfaces of ionotropic glutamate receptors.The Journal of physiology · 2015Review
- Structure and gating of tetrameric glutamate receptors.The Journal of physiology · 2015Review
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Authors and funding
5 authors.
Funding
Abstract
Kainate-selective ionotropic glutamate receptors (iGluRs) fulfil key roles in the CNS, making them the subject of detailed structural and functional analyses. Although they are known to gate a channel pore with high and low ion-permeation rates, it is still not clear how switches between these gating modes are achieved at the structural level. Here, we uncover an unexpected role for the ligand-binding domain (LBD) dimer assembly in this process. Covalent crosslinking of the dimer interface keeps kainate receptors out of the main open state but permits access to lower conductance states suggesting that significant rearrangements of the dimer interface are required for the receptor to achieve full activation. These observations differ from NMDA-selective iGluRs where constraining dimer movement reduces open-channel probability. In contrast, our data show that restricting movement of the dimer interface interferes with conformational changes that underlie both activation and desensitization. Working within the limits of a common architectural design, we propose functionally diverse iGluR families were able to emerge during evolution by re-deploying existing gating structures to fulfil different tasks.
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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.