ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
Glutamate receptor trafficking: endoplasmic reticulum quality control involves ligand binding and receptor function.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 85 citations in OpenAlex.
- Adapting the endoplasmic reticulum proteostasis rescues epilepsy-associated NMDA receptor variants.Acta pharmacologica Sinica · 2024Article
- An Insight into Animal Glutamate Receptors Homolog ofPlants (Basel, Switzerland) · 2022Review
- Synaptic Dysfunction by Mutations inBrain sciences · 2022Article
- Protein quality control ofFrontiers in cellular neuroscience · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3.The EMBO journal · 2020Article
- Cadmium opens GluK2 kainate receptors with cysteine substitutions at the M3 helix bundle crossing.The Journal of general physiology · 2019Article
- Assembly and Trafficking of Homomeric and Heteromeric Kainate Receptors with Impaired Ligand Binding Sites.Neurochemical research · 2019Article
- Holographic two-photon activation for synthetic optogenetics.Nature protocols · 2019Article
- Article
- Cognate Ligand Chaperoning: a Novel Mechanism for the Post-translational Regulation of Neurotransmitter Receptor Biogenesis.Frontiers in cellular neuroscience · 2017Article
- Mechanistic Insight into NMDA Receptor Dysregulation by Rare Variants in the GluN2A and GluN2B Agonist Binding Domains.American journal of human genetics · 2016Article
- Synaptic AMPA receptor composition in development, plasticity and disease.Nature reviews. Neuroscience · 2016Review
- Aggregation Limits Surface Expression of Homomeric GluA3 Receptors.The Journal of biological chemistry · 2016Article
- The Transmembrane Domain Mediates Tetramerization of α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors.The Journal of biological chemistry · 2016Article
- A Toolkit for Orthogonal and in vivo Optical Manipulation of Ionotropic Glutamate Receptors.Frontiers in molecular neuroscience · 2016Article
- Neuronal gamma-aminobutyric acid (GABA) type A receptors undergo cognate ligand chaperoning in the endoplasmic reticulum by endogenous GABA.Frontiers in cellular neuroscience · 2015Article
- Assembly of AMPA receptors: mechanisms and regulation.The Journal of physiology · 2015Review
- Contributions of different kainate receptor subunits to the properties of recombinant homomeric and heteromeric receptors.Neuroscience · 2014Article
- The neurotoxin domoate causes long-lasting inhibition of the kainate receptor GluK5 subunit.Neuropharmacology · 2014Article
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Authors and funding
4 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 domains in the N-terminal and M3-M4 loop regions, respectively. In the present study, we sought to confirm that the conserved ligand-binding residues identified in the AMPA receptor S1S2 domains also participate in ligand binding of GluR6 kainate receptors. Amino acid substitutions were made in the GluR6 parent at R523, T690, and E738 to alter their potential interactions with ligand. Mutant receptors were expressed in human embryonic kidney 293 cells, confirmed by Western blot analysis, and tested by [3H]kainate binding and patch-clamp recording. Each of the binding site mutations was sufficient to reduce [3H]kainate binding to undetectable levels and eliminate functional responses to glutamate or kainate. As with our studies of other nonfunctional mutants (Fleck et al., 2003), immunocytochemical staining and cell-surface biotinylation studies showed that the mutant receptors were retained intracellularly and did not traffic to the cell surface. Endoglycosidase-H digests and colocalization with endoplasmic reticulum (ER) markers demonstrated that the mutant receptors are immaturely glycosylated and retained in the ER. Immunoprecipitation, native PAGE, and functional studies confirmed that the GluR6-binding site mutants are capable of multimeric assembly, indicating their retention in the ER does not result from a gross protein folding error. Together, these results confirm the role of R523, T690, and E738 directly in ligand binding to GluR6 and further support our previous report that nonfunctional GluRs are retained intracellularly by a functional checkpoint in ER quality control.
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