Evidence map›Paper›PMID 29224722›Full record

ArticleNeuron2017

NRAP-1 Is a Presynaptically Released NMDA Receptor Auxiliary Protein that Modifies Synaptic Strength.

Ning Lei, Jerry E Mellem, Penelope J Brockie, David M Madsen, Andres V Maricq

Open access · bronzeAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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 · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. d-Serine and d-Alanine Regulate Adaptive Foraging Behavior inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  10. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ning LeiDepartment of Biology, Center for Cell and Genome Science, University of Utah, Salt Lake City, UT 84112-0840, USA.
Jerry E MellemDepartment of Biology, Center for Cell and Genome Science, University of Utah, Salt Lake City, UT 84112-0840, USA.
Penelope J BrockieDepartment of Biology, Center for Cell and Genome Science, University of Utah, Salt Lake City, UT 84112-0840, USA.
David M MadsenDepartment of Biology, Center for Cell and Genome Science, University of Utah, Salt Lake City, UT 84112-0840, USA.
Andres V MaricqDepartment of Biology, Center for Cell and Genome Science, University of Utah, Salt Lake City, UT 84112-0840, USA. Electronic address: maricq@biology.utah.edu.
University of Utah · US

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
Simultaneous in vivo studies of synapses, neurons, and learning and memoryDP1DA035080 · NIDA · UNIVERSITY OF UTAH · PI MARICQ, ANDRES VILLU · 2012 to 2014
$2.2M
NIDA NIH HHS DP1 DA035080NIH HHS P40 OD010440
6 · The paper itself

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.

Indexed as

AnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsGene Expression RegulationGlutamic AcidInterneuronsIon Channel GatingMembrane ProteinsMovementMuscle CellsMutationN-MethylaspartateNuclear ProteinsOocytesReceptors, N-Methyl-D-AspartateCaenorhabditis elegans ProteinsGlutamic AcidMembrane ProteinsN-MethylaspartateNMR-2 protein, C elegansnol-6 protein, C elegansNuclear ProteinsReceptors, N-Methyl-D-AspartateRecombinant ProteinsRNA-Binding Proteinsauxiliary proteinglutamateiGluRlearning and memoryNMDA receptorreceptor desensitizationsilent synapsesynaptic plasticity

Identifiers

PMID29224722
PMCPMC8819664
OpenAlexW2773380467

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.