ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Interface interactions modulating desensitization of the kainate-selective ionotropic glutamate receptor subunit GluR6.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 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
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Functional Validation of Heteromeric Kainate Receptor Models.Biophysical journal · 2017Article
- 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
- 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
- Crosslinking the ligand-binding domain dimer interface locks kainate receptors out of the main open state.The Journal of physiology · 2013Article
- Correlating efficacy and desensitization with GluK2 ligand-binding domain movements.Open biology · 2013Article
- Zinc potentiates GluK3 glutamate receptor function by stabilizing the ligand binding domain dimer interface.Neuron · 2012Article
- Distinct functional roles of subunits within the heteromeric kainate receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- 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
- 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
- Critical roles for the M3-S2 transduction linker domain in kainate receptor assembly and postassembly trafficking.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Ionotropic glutamate receptors from the AMPA and kainate subfamilies share many functional and structural features, but it is unclear whether this similarity extends to the molecular mechanisms underlying receptor desensitization. The current model for desensitization in AMPA receptors involves the rearrangement of dimers formed between subunit agonist binding domains. Key evidence for this has come from a single point mutant (from leucine to tyrosine) that abolished desensitization and that was shown to stabilize the binding domain dimer. However, the desensitization of kainate receptors appears to differ from that of AMPA receptors in several key respects. Although the kinetics of AMPA receptor gating and desensitization are consistent with channels formed from two dimers, similar evidence for the functional involvement of dimers has not been found in kainate receptors. Furthermore, despite the homolog of the nondesensitizing tyrosine in AMPA subunits also being a tyrosine in wild-type kainate subunits, these receptors desensitize rapidly and completely. Using mutagenesis based on the crystal structure of the glutamate receptor subunit GluR6 S1S2 domain in complex with domoate, we identified four residues neighboring this tyrosine that differ between AMPA and kainate subunits and that contribute to the different desensitization kinetics of these receptors. Detailed analysis of the effects of mutations at these sites confirms that there is in fact a common general mechanism for desensitization in non-NMDA receptors, dependent on the stability of the binding domain dimer interface, and reveals the existence of potential agonist-specific desensitization pathways.
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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.