Evidence map›Paper›PMID 22948148›Full record

ArticleThe Journal of biological chemistry2012

C-terminal domains of N-methyl-D-aspartic acid receptor modulate unitary channel conductance and gating.

Bruce A Maki, Teresa K Aman, Stacy A Amico-Ruvio, Cassandra L Kussius, Gabriela K Popescu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

37 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  3. Article
  4. Article
  5. Selective Cell-Surface Expression of Triheteromeric NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  6. Estimating the CaMethods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Article
  8. Article
  9. Membrane Stretch Gates NMDA Receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  10. Review
  11. Review
  12. Review
  13. Palmitoylation Controls NMDA Receptor Function and Steroid Sensitivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  14. Article
  15. Cross-subunit interactions that stabilize open states mediate gating in NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Review
  17. Review
  18. CaBiophysical journal · 2020
    Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Bruce A MakiNeuroscience Program, University at Buffalo, State University of New York, Buffalo, New York 14214, USA.
Teresa K Aman
Stacy A Amico-Ruvio
Cassandra L Kussius
Gabriela K Popescu
University at Buffalo, State University of New York · US

Funding

Probing allosteric surfaces of NMDA receptorsR01NS052669 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI POPESCU, GABRIELA K · 2006 to 2015
$3.4M
Permeation Mechanisms in NMDA receptorsR01NS097016 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI POPESCU, GABRIELA K · 2016 to 2019
$1.4M
NINDS NIH HHS R01 NS052669NINDS NIH HHS R01 NS097016PHS HHS NINDS 052669
6 · The paper itself

Abstract

NMDA receptors (NRs) are glutamate-gated calcium-permeable channels that are essential for normal synaptic transmssion and contribute to neurodegeneration. Tetrameric proteins consist of two obligatory GluN1 (N1) and two GluN2 (N2) subunits, of which GluN2A (2A) and GluN2B (2B) are prevalent in adult brain. The intracellularly located C-terminal domains (CTDs) make a significant portion of mass of the receptors and are essential for plasticity and excitotoxicity, but their functions are incompletely defined. Recent evidence shows that truncation of the N2 CTD alters channel kinetics; however, the mechanism by which this occurs is unclear. Here we recorded activity from individual NRs lacking the CTDs of N1, 2A, or 2B and determined the gating mechanisms of these receptors. Receptors lacking the N1 CTDs had larger unitary conductance and faster deactivation kinetics, receptors lacking the 2A or 2B CTDs had longer openings and longer desensitized intervals, and the first 100 amino acids of the N2 CTD were essential for these changes. In addition, receptors lacking the CTDs of either 2A or 2B maintained isoform-specific kinetic differences and swapping CTDs between 2A and 2B had no effect on single-channel properties. Based on these results, we suggest that perturbations in the CTD can modify the NR-mediated signal in a subunit-dependent manner, in 2A these effects are most likely mediated by membrane-proximal residues, and the isoform-specific biophysical properties conferred by 2A and 2B are CTD-independent. The kinetic mechanisms we developed afford a quantitative approach to understanding how the intracellular domains of NR subunits can modulate the responses of the receptor.

Indexed as

AnimalsHEK293 CellsHumansIon Channel GatingKineticsProtein IsoformsProtein Structure, TertiaryRatsReceptors, N-Methyl-D-AspartateProtein IsoformsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID22948148
PMCPMC3476275
OpenAlexW2068653092

What OpenQuestion holds

Textmetadata
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.