ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
NR3A modulates the outer vestibule of the "NMDA" receptor channel.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Structural and mechanistic insights into gating and allosteric modulation of GluN1-GluN3A NMDA receptors.Nature structural & molecular biology · 2026Article
- Extrasynaptic NMDA receptors in acute and chronic excitotoxicity: implications for preventive treatments of ischemic stroke and late-onset Alzheimer's disease.Molecular neurodegeneration · 2023Review
- A role for endothelial NMDA receptors in the pathophysiology of schizophrenia.Schizophrenia research · 2022Review
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Negative allosteric modulation of GluN1/GluN3 NMDA receptors.Neuropharmacology · 2020Article
- Residues in the GluN1 C-terminal domain control kinetics and pharmacology of GluN1/GluN3A N-methyl-d-aspartate receptors.Neuropharmacology · 2017Article
- NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017Article
- An NMDA receptor gating mechanism developed from MD simulations reveals molecular details underlying subunit-specific contributions.Biophysical journal · 2013Article
- Key binding interactions for memantine in the NMDA receptor.ACS chemical neuroscience · 2013Article
- GluN3A: an NMDA receptor subunit with exquisite properties and functions.Neural plasticity · 2013Review
- Article
- N-methyl-D-aspartate receptor subunit NR3a expression and function in principal cells of the collecting duct.American journal of physiology. Renal physiology · 2011Article
- Residues at the tip of the pore loop of NR3B-containing NMDA receptors determine Ca2+ permeability and Mg2+ block.BMC neuroscience · 2010Article
- Glutamate receptor ion channels: structure, regulation, and function.Pharmacological reviews · 2010Review
- Influence of the NR3A subunit on NMDA receptor functions.Progress in neurobiology · 2010Review
- Potentiation of Glycine-Gated NR1/NR3A NMDA Receptors Relieves Ca-Dependent Outward Rectification.Frontiers in molecular neuroscience · 2010Article
- Calpain and the glutamatergic synapse.Frontiers in bioscience (Scholar edition) · 2009Review
- Effects of NR1 splicing on NR1/NR3B-type excitatory glycine receptors.BMC neuroscience · 2009Article
- Shuffling the deck anew: how NR3 tweaks NMDA receptor function.Molecular neurobiology · 2008Review
- Subunit-specific contribution of pore-forming domains to NMDA receptor channel structure and gating.The Journal of general physiology · 2007Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Classical NMDA receptors (NMDARs), activated by glycine and glutamate, are heteromultimers comprised of NR1 and NR2 subunits. Coexpression of the novel NR3 family of NMDAR subunits decreases the magnitude of NR1/NR2 receptor-mediated currents or forms glycine-activated channels with the NR1 subunit alone. The second (M2) and third (M3) membrane segments of NR1 and NR2 subunits of classical NMDARs form the core of the channel permeation pathway. Structural information regarding NR1/NR3 channels remains unknown. Using the Xenopus oocyte expression system and the SCAM (substituted cysteine accessibility method), we found that M3 segments of both NR1 and NR3A form a narrow constriction in the outer vestibule of the channel, which prevents passage of externally applied sulfhydryl-specific agents. The most internal reactive residue in each M3 segment is the threonine in the conserved SYTANLAAF motif. These threonines appear to be symmetrically aligned. Several NR3A M3 mutations change the behavior of NR1/NR3A channels. Unlike NR1, however, the M3 segment of NR3A does not undergo extensive molecular rearrangement during channel gating by added glycine. Additionally, in the M2 segment, our data suggest that the amino acid at the asparagine (N) site of NR1, but not NR3A, contributes to the selectivity filter of NR1/3A channels. We therefore conclude that NR3A modulates the NR1/NR3A permeation pathway via a novel mechanism of forming a narrow constriction at the outer channel vestibule. This modified channel vestibule may also explain the dominant-negative effect of the NR3 subunit on channel behavior when coexpressed with NR1 and NR2 subunits.
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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.