ArticleNature communications2020
Positive surface charge of GluN1 N-terminus mediates the direct interaction with EphB2 and NMDAR mobility.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- EphB1-NR2B receptor signaling in glutamatergic neurons of the ventroposteromedial thalamic nucleus regulates emergence from anesthesia.Science advances · 2025Article
- Effects and Mechanisms of NMDAR-EphB2 on Synapses in Mice by Active Immunization with a GluN1 Peptide.Molecular neurobiology · 2025Article
- EphB2 receptor tyrosine kinase-mediated excitatory synaptic functions are negatively modulated by MDGA2.Progress in neurobiology · 2025Article
- EFNA4-enhanced deubiquitination of SLC7A11 inhibits ferroptosis in hepatocellular carcinoma.Apoptosis : an international journal on programmed cell death · 2025Article
- Peptide-Purified Anti-N-methyl-D-aspartate Receptor (NMDAR) Autoantibodies Have Inhibitory Effect on Long-Term Synaptic Plasticity.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024Review
- ephrin-B2 promotes nociceptive plasticity and hyperalgesic priming through EphB2-MNK-eIF4E signaling in both mice and humans.Pharmacological research · 2024Article
- NMDA receptor autoantibodies primarily impair the extrasynaptic compartment.Brain : a journal of neurology · 2024Article
- Individual NMDA receptor GluN2 subunit signaling domains differentially regulate the postnatal maturation of hippocampal excitatory synaptic transmission and plasticity but not dendritic morphology.Synapse (New York, N.Y.) · 2024Article
- VLK drives extracellular phosphorylation of EphB2 to govern the EphB2-NMDAR interaction and injury-induced pain.bioRxiv : the preprint server for biology · 2024Article
- Loss of postsynaptic NMDARs drives nanoscale reorganization of Munc13-1 and PSD-95.bioRxiv : the preprint server for biology · 2024Article
- Impaired erythropoietin-producing hepatocellular B receptors signaling in the prefrontal cortex and hippocampus following maternal immune activation in male rats.Genes, brain, and behavior · 2023Article
- GluN3A subunit tunes NMDA receptor synaptic trafficking and content during postnatal brain development.Cell reports · 2023Article
- Nanoscale rules governing the organization of glutamate receptors in spine synapses are subunit specific.Nature communications · 2022Article
- Regulation of NMDA Receptor Signaling at Single Synapses by Human Anti-NMDA Receptor Antibodies.Frontiers in molecular neuroscience · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Regulation of membrane NMDA receptors by dynamics and protein interactions.The Journal of cell biology · 2021Review
- Roles of N-Methyl-D-Aspartate Receptors (NMDARs) in Epilepsy.Frontiers in molecular neuroscience · 2021Review
- Anti-NMDA receptor encephalitis: a review of mechanistic studies.International journal of physiology, pathophysiology and pharmacology · 2021Review
- Synaptic recognition molecules in development and disease.Current topics in developmental biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Localization of the N-methyl-D-aspartate type glutamate receptor (NMDAR) to dendritic spines is essential for excitatory synaptic transmission and plasticity. Rather than remaining trapped at synaptic sites, NMDA receptors undergo constant cycling into and out of the postsynaptic density. Receptor movement is constrained by protein-protein interactions with both the intracellular and extracellular domains of the NMDAR. The role of extracellular interactions on the mobility of the NMDAR is poorly understood. Here we demonstrate that the positive surface charge of the hinge region of the N-terminal domain in the GluN1 subunit of the NMDAR is required to maintain NMDARs at dendritic spine synapses and mediates the direct extracellular interaction with a negatively charged phospho-tyrosine on the receptor tyrosine kinase EphB2. Loss of the EphB-NMDAR interaction by either mutating GluN1 or knocking down endogenous EphB2 increases NMDAR mobility. These findings begin to define a mechanism for extracellular interactions mediated by charged domains.
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Registered trials
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.