ArticleNature communications2025
Trans-synaptic molecular context of NMDA receptor nanodomains.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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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
7 citing papers in PubMed.
- The AMPA receptor life cycle: assembly, regulation and synaptic diversity.Nature reviews. Neuroscience · 2026Review
- Btbd11 regulates glutamatergic synapse organization in GABAergic inhibitory interneurons.bioRxiv : the preprint server for biology · 2026Article
- Molecular Physiology of the Neuronal Synapse.Current issues in molecular biology · 2026Review
- A general one-step protocol to generate impermeable fluorescent HaloTag substrates for in situ live cell application and super-resolution imaging.Nature communications · 2026Article
- Novel binding mode for negative allosteric NMDA receptor modulators.The Journal of general physiology · 2026Article
- Trans-synaptic molecular context of NMDA receptor nanodomains.Nature communications · 2025Article
- Loss of postsynaptic NMDARs drives nanoscale reorganization of Munc13-1 and PSD-95.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Tight coordination of spatial relationships between protein complexes is required for cellular function. In neuronal synapses, proteins responsible for neurotransmission form subsynaptic nanoclusters whose trans-cellular alignment modulates synaptic signal propagation. However, the spatial relationships between these proteins and NMDA receptors (NMDARs), which are required for learning and memory, remain undefined. Here, we mapped key NMDAR subunits relative to active zone and post-synaptic density reference proteins using multiplexed super-resolution DNA-PAINT microscopy in rat hippocampal neurons. GluN2A and GluN2B subunits formed diverse nanoclusters that, surprisingly, were not localized near presynaptic vesicle release sites marked by Munc13-1. However, a subset of release sites was enriched with NMDARs, and modeling indicated this nanotopography promotes NMDAR activation. These enriched sites were internally denser with Munc13-1, aligned with PSD-95, and closely associated with specific NMDAR nanodomains. NMDAR activation rapidly reorganized this relationship, suggesting a structural mechanism for tuning NMDAR-mediated synaptic transmission. These findings suggest synaptic functional architecture depends on assembly of and trans-cellular spatial relationships between multiprotein nanodomains.
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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 Socratic graph.