ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
Distinct functional roles of subunits within the heteromeric kainate receptor.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 44 citations in OpenAlex.
- Cryo-EM structures of apo, agonist- and antagonist-bound heteromeric kainate receptors.Science advances · 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
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Partial agonism in heteromeric GLUK2/GLUK5 kainate receptor.Proteins · 2025Article
- Behavioral analysis of kainate receptor KO mice and the role of GluK3 subunit in anxiety.Scientific reports · 2024Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Clustered mutations in the GRIK2 kainate receptor subunit gene underlie diverse neurodevelopmental disorders.American journal of human genetics · 2021Article
- Article
- Subunit-selective iGluR antagonists can potentiate heteromeric receptor responses by blocking desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cadmium activates AMPA and NMDA receptors with M3 helix cysteine substitutions.The Journal of general physiology · 2020Article
- Review
- Does kynurenic acid act on nicotinic receptors? An assessment of the evidence.Journal of neurochemistry · 2020Review
- The structural arrangement and dynamics of the heteromeric GluK2/GluK5 kainate receptor as determined by smFRET.Biochimica et biophysica acta. Biomembranes · 2020Article
- Development of Cortical Pyramidal Cell and Interneuronal Dendrites: a Role for Kainate Receptor Subunits and NETO1.Molecular neurobiology · 2019Article
- Assembly and Trafficking of Homomeric and Heteromeric Kainate Receptors with Impaired Ligand Binding Sites.Neurochemical research · 2019Article
- Kainate Receptors Play a Role in Modulating Synaptic Transmission in the Olfactory Bulb.Neuroscience · 2018Article
- Functional Validation of Heteromeric Kainate Receptor Models.Biophysical journal · 2017Article
- Dual Effects of TARP γ-2 on Glutamate Efficacy Can Account for AMPA Receptor Autoinactivation.Cell reports · 2017Article
- The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.Scientific reports · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Kainate receptors (KARs) have been implicated in a number of neurological disorders, including epilepsy. KARs are tetrameric, composed of a combination of GluK1-GluK5 subunits. We examined the contribution of GluK2 and GluK5 subunits to activation and desensitization of the heteromeric receptor. Heteromeric GluK2/K5 receptors expressed in HEK-293T cells showed markedly higher glutamate sensitivity than GluK2 homomers and did not desensitize at low glutamate concentrations. Mutation of residue E738 in GluK2 substantially lowered its glutamate sensitivity. However, heteromeric KARs containing this mutant GluK2 [GluK2(E738D)] assembled with wild-type GluK5 showed no change in glutamate EC(50) compared with wild-type heteromeric KARs. Instead, higher concentrations of glutamate were required to produce desensitization. This suggested that, within the heteromeric receptor, glutamate binding to the high-affinity GluK5 subunit alone was sufficient for channel activation but not desensitization, whereas agonist binding to the low-affinity GluK2 subunit was not necessary to open the channel but instead caused the channel to enter a closed, desensitized state. To test this hypothesis in wild-type receptors, we used the competitive antagonist kynurenate, which has higher affinity for the GluK2 than the GluK5 subunit. Coapplication of kynurenate with glutamate to heteromeric receptors reduced the onset of desensitization without affecting the peak current response, consistent with our hypothesis. Our results suggest that GluK2 and GluK5 subunits can be individually activated within the heteromeric receptor and that these subunits serve dramatically different functional roles.
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