Evidence map›Paper›PMID 28384476›Full record

ArticleNeuron2017

Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties.

Weinan Sun, Kasper B Hansen, Craig E Jahr

Abstract 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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Selective Cell-Surface Expression of Triheteromeric NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  11. Article
  12. Therapeutic potential of N-methyl-D-aspartate receptor modulators in psychiatry.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2024
    Review
  13. Article
  14. Article
  15. Synaptic NMDA receptor activity at resting membrane potentials.Frontiers in cellular neuroscience · 2022
    Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article
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

3 authors.

Weinan SunVollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Rd., Portland, OR 97239, USA.
Kasper B HansenDepartment of Biomedical and Pharmaceutical Sciences, University of Montana, 32 Campus Dr., Missoula, MT 59812, USA.
Craig E JahrVollum Institute, Oregon Health & Science University, 3181 SW Sam Jackson Park Rd., Portland, OR 97239, USA. Electronic address: jahr@ohsu.edu.

Funding

Surveillance genome sequencing to detect SARS-CoV-2 virus variants in MontanaP20GM103546 · NIGMS · UNIVERSITY OF MONTANA · PI BOWLER, BRUCE E · 2012 to 2021
$19.2M
Structural and functional investigation of negative allosteric NMDA receptor modulationR01NS097536 · NINDS · UNIVERSITY OF MONTANA · PI Kasper Boe Hansen · 2016 to 2026
$3.4M
Properties of Singly-Bound NMDA receptorsR21NS091337 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI JAHR, CRAIG E · 2015 to 2016
$424k
NIGMS NIH HHS P20 GM103546NINDS NIH HHS R01 NS097536NINDS NIH HHS R21 NS091337
6 · The paper itself

Abstract

During development of the central nervous system, there is a shift in the subunit composition of NMDA receptors (NMDARs) resulting in a dramatic acceleration of NMDAR-mediated synaptic currents. This shift coincides with upregulation of the GluN2A subunit and triheteromeric GluN1/2A/2B receptors with fast deactivation kinetics, whereas expression of diheteromeric GluN1/2B receptors with slower deactivation kinetics is decreased. Here, we show that allosteric interactions occur between the glutamate-binding GluN2 subunits in triheteromeric GluN1/2A/2B NMDARs. This allosterism is dominated by the GluN2A subunit and results in functional properties not predicted by those of diheteromeric GluN1/2A and GluN1/2B NMDARs. These findings suggest that GluN1/2A/2B NMDARs may maintain some signaling properties of the GluN2B subunit while having the kinetic properties of GluN1/2A NMDARs and highlight the complexity in NMDAR signaling created by diversity in subunit composition.

Indexed as

Gene Expression Regulation, DevelopmentalAllosteric RegulationAnimalsEndoplasmic ReticulumGlutamic AcidHEK293 CellsHumansNeuronal PlasticityOocytesPatch-Clamp TechniquesProtein SubunitsRatsReceptors, N-Methyl-D-AspartateSynaptic TransmissionXenopus laevisGlutamic AcidNR2B NMDA receptorProtein SubunitsReceptors, N-Methyl-D-Aspartateallosteric interactionamino-terminal domaincrosslinkingexcitatory synaptic transmissionGluN2 subunitglutamateopen probabilityreceptor deactivationTriheteromeric NMDA receptors

Identifiers

PMID28384476
PMCPMC5391998

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Registered trials

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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.