Evidence map›Paper›PMID 25393018›Full record

ArticlePloS one2014

FRET-FLIM investigation of PSD95-NMDA receptor interaction in dendritic spines; control by calpain, CaMKII and Src family kinase.

Kim Doré, Simon Labrecque, Christian Tardif, Paul De Koninck

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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  14. Agonist binding to the NMDA receptor drives movement of its cytoplasmic domain without ion flow.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

4 authors at 2 institutions in 1 country.

Kim DoréInstitut Universitaire en Santé Mentale de Québec, Université Laval, Québec, QC, Canada.
Simon LabrecqueInstitut Universitaire en Santé Mentale de Québec, Université Laval, Québec, QC, Canada.
Christian TardifInstitut Universitaire en Santé Mentale de Québec, Université Laval, Québec, QC, Canada.
Paul De KoninckInstitut Universitaire en Santé Mentale de Québec, Université Laval, Québec, QC, Canada; Département de Biochimie, Microbiologie et Bio-informatique, Université Laval, Québec, QC, Canada.
Institut Universitaire en Santé Mentale de Québec · CAUniversité Laval · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Little is known about the changes in protein interactions inside synapses during synaptic remodeling, as their live monitoring in spines has been limited. We used a FRET-FLIM approach in developing cultured rat hippocampal neurons expressing fluorescently tagged NMDA receptor (NMDAR) and PSD95, two essential proteins in synaptic plasticity, to examine the regulation of their interaction. NMDAR stimulation caused a transient decrease in FRET between the NMDAR and PSD95 in spines of young and mature neurons. The activity of both CaMKII and calpain were essential for this effect in both developmental stages. Meanwhile, inhibition of Src family kinase (SFK) had opposing impacts on this decrease in FRET in young versus mature neurons. Our data suggest concerted roles for CaMKII, SFK and calpain activity in regulating activity-dependent separation of PSD95 from GluN2A or GluN2B. Finally, we found that calpain inhibition reduced spine growth that was caused by NMDAR activity, supporting the hypothesis that PSD95-NMDAR separation is implicated in synaptic remodeling.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2CalpainCells, CulturedDendritic SpinesDisks Large Homolog 4 ProteinFluorescence Resonance Energy TransferHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsNeuronal PlasticityRatsReceptors, N-Methyl-D-AspartateSignal Transductionsrc-Family KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2CalpainDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMembrane ProteinsNR2B NMDA receptorReceptors, N-Methyl-D-Aspartatesrc-Family Kinases

Identifiers

PMID25393018
PMCPMC4230936
OpenAlexW2030487055

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.