Evidence map›Paper›PMID 22761831›Full record

ArticlePloS one2012

Trafficking of the NMDAR2B receptor subunit distal cytoplasmic tail from endoplasmic reticulum to the synapse.

Steve Standley, Ronald S Petralia, Manneth Gravell, Rebecca Hamilton, Ya-Xian Wang, Manfred Schubert, Robert J Wenthold

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Protein quality control ofFrontiers in cellular neuroscience · 2022
    Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. NMDA receptors are upregulated and trafficked to the plasma membrane after sigma-1 receptor activation in the rat hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  11. ER to synapse trafficking of NMDA receptors.Frontiers in cellular neuroscience · 2014
    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

7 authors at 3 institutions in 1 country.

Steve StandleyGraduate College of Biomedical Sciences, Western University of Health Sciences, Pomona, California, United States of America. sstandley@westernu.edu
Ronald S Petralia
Manneth Gravell
Rebecca Hamilton
Ya-Xian Wang
Manfred Schubert
Robert J Wenthold
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · USWestern University of Health Sciences · US

Funding

Advanced Imaging CoreZICDC000081 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI WINKLER, DENNIS · 2012 to 2025
$17.4M
Molecular Mechanisms Of Synaptic TransmissionZIADC000003 · NIDCD · NATIONAL INSTITUTE ON DEAFNESS AND OTHER COMMUNICATION DISORDERS · PI ROBINSON, DAVID · 2009 to 2012
$6.3M
Gene Delivery To The Nervous SystemZIANS002997 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SCHUBERT, MANFRED H · 2009 to 2019
$1.9M
Intramural NIH HHS
6 · The paper itself

Abstract

NMDA receptor NR2A/B subunits have PDZ-binding domains on their extreme C-termini that are known to interact with the PSD-95 family and other PDZ proteins. We explore the interactions between PSD-95 family proteins and the NR2A/B cytoplasmic tails, and the consequences of these interactions, from the endoplasmic reticulum (ER) through delivery to the synapse in primary rat hippocampal and cortical cultured neurons. We find that the NR2A/B cytoplasmic tails cluster very early in the secretory pathway and interact serially with SAP102 beginning at the intermediate compartment, and then PSD-95. We further establish that colocalization of the distal C-terminus of NR2B and PSD-95 begins at the trans-Golgi Network (TGN). Formation of NR2B/PSD-95/SAP102 complexes is dependent on the PDZ binding domain of NR2B subunits, but association with SAP102 and PSD-95 plays no distinguishable role in cluster pre-formation or initial targeting to the vicinity of the synapse. Instead the PDZ binding domain plays a role in restricting cell-surface clusters to postsynaptic targets.

Indexed as

AnimalsCells, CulturedCerebral CortexDisks Large Homolog 4 ProteinEndoplasmic ReticulumHippocampusIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeuronsProtein TransportRatsReceptors, N-Methyl-D-AspartateSynapsesDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMembrane ProteinsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID22761831
PMCPMC3384676
OpenAlexW2043998746

What OpenQuestion holds

Textmetadata
LicenceCC0
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.