ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009
Modulation of the dimer interface at ionotropic glutamate-like receptor delta2 by D-serine and extracellular calcium.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 60 citations in OpenAlex.
- GluD1 is localized at cholinergic synapses and is an acetylcholine receptor.Molecular psychiatry · 2026Article
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- N-Methyl-D-aspartate receptors: structure, signaling and roles in atherosclerosis.Journal of translational medicine · 2026Review
- GluDs are ionotropic dopamine receptors tuned by G-proteins.bioRxiv : the preprint server for biology · 2026Article
- Molecular basis for ligand-gating of the human GluD1 receptor.bioRxiv : the preprint server for biology · 2026Article
- Article
- D-Serine disrupts Cbln1 and GluD1 interaction and affects Cbln1-dependent synaptic effects and nocifensive responses in the central amygdala.Cellular and molecular life sciences : CMLS · 2025Article
- The spiny relationship between parallel fibers, climbing fibers, and Purkinje cells.Frontiers in physiology · 2025Review
- Lack of evidence for direct ligand-gated ion channel activity of GluD receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Loss of activation by GABA in vertebrate delta ionotropic glutamate receptors.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Clinical features, functional consequences, and rescue pharmacology of missense GRID1 and GRID2 human variants.Human molecular genetics · 2024Article
- An unexpected role for a glutamate receptor.Science (New York, N.Y.) · 2023Article
- Potentiation of neuronal activity by tonic GluD1 current in brain slices.EMBO reports · 2023Article
- GluD receptors are functional ion channels.Biophysical journal · 2023Review
- Delta glutamate receptors are functional glycine- and ᴅ-serine-gated cation channels in situ.Science advances · 2021Article
- Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- An emerging map of glutamate delta 1 receptors in the forebrain.Neuropharmacology · 2021Review
- Structural biology and thermodynamics of GluD receptors.Neuropharmacology · 2021Review
- Article
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7 authors at 2 institutions in 2 countries.
Funding
Abstract
GluRdelta2 is a member of the iGluR family, but despite a prominent role in cerebellar synaptic plasticity, this receptor does not appear to function as an ion channel. Endogenous ligands that modulate the activity of native GluRdelta2 in the cerebellum have not been identified, but two candidate modulators are d-serine and extracellular calcium. Taking advantage of known crystal structures and spontaneously active GluRdelta2 receptors containing the lurcher mutation (GluRdelta2(Lc)), we investigated the mechanism by which calcium and d-serine regulate the activity of GluRdelta2(Lc). Our data suggest that calcium binding stabilizes the dimer interface formed between two agonist-binding domains and increases GluRdelta2(Lc) currents. The data further suggest that d-serine binding induces rearrangements at the dimer interface to diminish GluRdelta2(Lc) currents by a mechanism that resembles desensitization at AMPA and kainate receptors. Thus, we propose that calcium and d-serine binding have opposing effects on the stability of the dimer interface. Furthermore, the effects of calcium are observed at concentrations that are within the physiological range, suggesting that the ability of native GluRdelta2 to respond to ligand binding may be modulated by extracellular calcium. These findings place GluRdelta2 among AMPA and kainate receptors, where the dimer interface is not only a biologically important site for functional regulation, but also an important target for exogenous and endogenous ligands that modulate receptor function.
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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.