ArticleNeuron2017
NRAP-1 Is a Presynaptically Released NMDA Receptor Auxiliary Protein that Modifies Synaptic Strength.
Article in Neuron, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- The insulin-like peptide INS-27 mediates a muscle-to-neuron feedback signal coupling muscle activity with AMPA receptor trafficking.PLoS genetics · 2025Article
- Alternating electric fields transform the intricate network of tumour vasculature into orderly parallel capillaries and enhance the anti-angiogenesis effect of bevacizumab.Cell proliferation · 2025Article
- Mechanistic and structural studies reveal NRAP-1-dependent coincident activation of NMDARs.Cell reports · 2024Article
- Article
- An extracellular scaffolding complex confers unusual rectification upon an ionotropic acetylcholine receptor inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- MAPK signaling and a mobile scaffold complex regulate AMPA receptor transport to modulate synaptic strength.Cell reports · 2022Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- Targeting receptor complexes: a new dimension in drug discovery.Nature reviews. Drug discovery · 2020Review
- d-Serine and d-Alanine Regulate Adaptive Foraging Behavior inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Article
- Subsynaptic spatial organization as a regulator of synaptic strength and plasticity.Current opinion in neurobiology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
NMDA receptors (NMDARs) are a subtype of postsynaptic ionotropic glutamate receptors that function as molecular coincidence detectors, have critical roles in models of learning, and are associated with a variety of neurological and psychiatric disorders. To date, no auxiliary proteins that modify NMDARs have been identified. Here, we report the identification of NRAP-1, an auxiliary protein in C. elegans that modulates NMDAR function. NMDAR-mediated currents were eliminated in nrap-1 mutants, as was NMDA-dependent behavior. We show that reconstitution of NMDA-gated current in Xenopus oocytes, or C. elegans muscle cells, depends on NRAP-1 and that recombinant NRAP-1 can convert silent NMDARs to functional channels. Our data indicate that NRAP-1, secreted from presynaptic neurons, localizes to glutamatergic synapses, where it associates with postsynaptic NMDARs to modify receptor gating. Thus, our studies reveal a novel mechanism for synaptic regulation via pre-synaptic control of NMDAR-mediated synaptic transmission.
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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.