ArticleThe Journal of physiology2006
Concanavalin-A reports agonist-induced conformational changes in the intact GluR6 kainate receptor.
Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Structural basis of GluK2 kainate receptor activation by a partial agonist.Nature structural & molecular biology · 2025Article
- Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Structural Arrangement Produced by Concanavalin A Binding to Homomeric GluK2 Receptors.Membranes · 2021Article
- Animal Galectins and Plant Lectins as Tools for Studies in Neurosciences.Current neuropharmacology · 2020Review
- Neto proteins regulate gating of the kainate-type glutamate receptor GluK2 through two binding sites.The Journal of biological chemistry · 2019Article
- N-glycan content modulates kainate receptor functional properties.The Journal of physiology · 2017Article
- ConBr, A Lectin Purified from the Seeds of Canavalia brasiliensis, Protects Against Ischemia in Organotypic Culture of Rat Hippocampus: Potential Implication of Voltage-Gated Calcium Channels.Neurochemical research · 2017Article
- Modulation of ionotropic glutamate receptor function by vertebrate galectins.The Journal of physiology · 2014Article
- The role of protein N-glycosylation in neural transmission.Glycobiology · 2014Review
- Vatairea macrocarpa lectin (VML) induces depressive-like behavior and expression of neuroinflammatory markers in mice.Neurochemical research · 2013Article
- On the ligand binding profile and desensitization of plant ionotropic glutamate receptor (iGluR)-like channels functioning in MAMP-triggered Ca²⁺ influx.Plant signaling & behavior · 2012Article
- Structure of a tetrameric galectin from Cinachyrella sp. (ball sponge).Acta crystallographica. Section D, Biological crystallography · 2012Article
- ConBr, a lectin from Canavalia brasiliensis seeds, protects against quinolinic acid-induced seizures in mice.Neurochemical research · 2012Article
- Cations but not anions regulate the responsiveness of kainate receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Na+/Cl- dipole couples agonist binding to kainate receptor activation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Interface interactions modulating desensitization of the kainate-selective ionotropic glutamate receptor subunit GluR6.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- N-glycosylation in regulation of the nervous system.Advances in neurobiologyArticle
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The agonist-binding domain of ionotropic glutamate receptors (iGluRs) has recently been crystallized as two polypeptide chains with a linker region. Although work on the structure of this isolated ligand-binding core has been invaluable, there is debate over how it relates to conformations adopted by intact receptors. iGluR crystals are proposed to represent the activated state as their degree of domain closure correlates well with agonist efficacy. However, iGluR crystals exhibit high agonist affinity that more closely matches that of desensitized receptors. Consequently, conformations adopted by iGluR crystals may represent this state. To test this, we have employed the plant lectin, concanavalin-A (Con-A) to report conformational changes elicited by kainate (KA) iGluR agonists during desensitization. When GluR6 KA receptors (KARs) were pre-incubated with Con-A, equilibrium responses evoked by the full agonist, l-glutamate (l-Glu), increased almost 30-fold. However, in the continued presence of l-Glu, Con-A exerted no effect suggesting that it has restricted access to its binding sites when the agonist is bound. However, Con-A does not discriminate well between agonist-bound or -unbound states with the weak partial agonist, domoate. Accessibility experiments with KA were intermediate in nature consistent with its equilibrium efficacy at GluR6 KARs. Our results suggest that full and partial agonists elicit distinct conformational changes in KARs during desensitization. This finding can be reconciled with crystallographic data if the agonist-binding domain adopts the same conformation in the activated and desensitized states. However, other interpretations are possible suggesting future work is required if this issue is to be resolved.
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