ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2003
Amino-acid residues involved in glutamate receptor 6 kainate receptor gating and desensitization.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2003. 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, 68 citations in OpenAlex.
- 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
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Assembly and Trafficking of Homomeric and Heteromeric Kainate Receptors with Impaired Ligand Binding Sites.Neurochemical research · 2019Article
- Article
- Retour aux sources: defining the structural basis of glutamate receptor activation.The Journal of physiology · 2015Review
- Agonist binding to the GluK5 subunit is sufficient for functional surface expression of heteromeric GluK2/GluK5 kainate receptors.Cellular and molecular neurobiology · 2013Article
- Modulation of GluK2a subunit-containing kainate receptors by 14-3-3 proteins.The Journal of biological chemistry · 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
- Transmembrane region of N-methyl-D-aspartate receptor (NMDAR) subunit is required for receptor subunit assembly.The Journal of biological chemistry · 2011Article
- Cations but not anions regulate the responsiveness of kainate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- The biochemistry, ultrastructure, and subunit assembly mechanism of AMPA receptors.Molecular neurobiology · 2010Review
- Control of assembly and function of glutamate receptors by the amino-terminal domain.Molecular pharmacology · 2010Review
- 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
- Vibrational spectroscopic investigation of the ligand binding domain of kainate receptors.Protein science : a publication of the Protein Society · 2009Article
- Glutamate binding and conformational flexibility of ligand-binding domains are critical early determinants of efficient kainate receptor biogenesis.The Journal of biological chemistry · 2009Article
- Stability of ligand-binding domain dimer assembly controls kainate receptor desensitization.The EMBO journal · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The glutamate receptor (GluR) agonist-binding site consists of amino acid residues in the extracellular S1 and S2 segments in the N-terminal and M3-M4 loop regions, respectively. Molecular and atomic level structural analyses have identified specific S1 and S2 residues that interact directly with ligands, interact with one another in a dimeric configuration, and influence channel gating and desensitization properties of AMPA receptors. Other studies suggest that KA receptor gating and desensitization may differ mechanistically. In particular, a leucine (L) to tyrosine (Y) mutation in the S1 segment of AMPA receptors is sufficient to block desensitization, whereas KA receptors naturally contain a tyrosine residue at the equivalent position (Y751 in GluR6) but retain the fast-desensitizing phenotype. We hypothesized that KA receptor desensitization is preserved by a compensatory substitution in the S2 segment. We generated a series of GluR6 mutants that converted individual S2 domain residues to their AMPA receptor equivalents. Various S2 mutations had effects on the kinetics of desensitization and recovery from desensitization, but no single amino acid substitution was found to block desensitization, as in the L/Y mutant AMPA receptors, or to prevent desensitization to KA. Other mutations designed to neutralize residues thought to interact across the dimer interface had dramatic effects on channel gating and desensitization. These results are consistent with a close but imperfect structural homology between AMPA and KA receptors and support the role of conserved S1S2 domain interactions at the dimer interface in GluR channel function.
Indexed as
Identifiers
12598610PMC6742261W2149390741What OpenQuestion holds
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.