Evidence map›Paper›PMID 26679993›Full record

ArticleNature communications2015

Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex.

Jennifer Stanic, Mario Carta, Ivano Eberini, Silvia Pelucchi, Elena Marcello, Armando A Genazzani, Claudia Racca, Christophe Mulle, Monica Di Luca, Fabrizio Gardoni

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

45 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Hyperfunction of PSD-95 leads to hyperexcitability and cognitive abnormalities in MEF2C haploinsufficiency.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

10 authors at 4 institutions in 3 countries.

Jennifer StanicDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
Mario CartaInstitut Interdisciplinaire de Neurosciences, University of Bordeaux, CNRS UMR 5297, Bordeaux 33000, France.
Ivano EberiniDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
Silvia PelucchiDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
Elena MarcelloDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
Armando A GenazzaniDipartimento di Scienze del Farmaco, Università degli Studi del Piemonte Orientale 'Amedeo Avogadro', Novara 28100, Italy.
Claudia RaccaInstitute of Neuroscience, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
Christophe MulleInstitut Interdisciplinaire de Neurosciences, University of Bordeaux, CNRS UMR 5297, Bordeaux 33000, France.
Monica Di LucaDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
Fabrizio GardoniDiSFeB, Dipartimento di Scienze Farmacologiche e Biomolecolari, Università degli Studi di Milano, Via Balzaretti 9, Milano 20133, Italy.
University of Milan · ITInstitut Interdisciplinaire de Neuroscience · FRNewcastle University · GBUniversità degli Studi del Piemonte Orientale “Amedeo Avogadro” · IT

Funding

Medical Research Council MR/J013250/1
6 · The paper itself

Abstract

NMDA receptor (NMDAR) composition and synaptic retention represent pivotal features in the physiology and pathology of excitatory synapses. Here, we identify Rabphilin 3A (Rph3A) as a new GluN2A subunit-binding partner. Rph3A is known as a synaptic vesicle-associated protein involved in the regulation of exo- and endocytosis processes at presynaptic sites. We find that Rph3A is enriched at dendritic spines. Protein-protein interaction assays reveals that Rph3A N-terminal domain interacts with GluN2A(1349-1389) as well as with PSD-95(PDZ3) domains, creating a ternary complex. Rph3A silencing in neurons reduces the surface localization of synaptic GluN2A and NMDAR currents. Moreover, perturbing GluN2A/Rph3A interaction with interfering peptides in organotypic slices or in vivo induces a decrease of the amplitude of NMDAR-mediated currents and GluN2A density at dendritic spines. In conclusion, Rph3A interacts with GluN2A and PSD-95 forming a complex that regulates NMDARs stabilization at postsynaptic membranes.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCA1 Region, HippocampalChlorocebus aethiopsComputer SimulationCOS CellsDendritic SpinesDisks Large Homolog 4 ProteinEndocytosisGuanylate KinasesHippocampusImmunohistochemistryImmunoprecipitationIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceAdaptor Proteins, Signal TransducingDisks Large Homolog 4 ProteinDlg4 protein, mouseDlg4 protein, ratGuanylate KinasesIntracellular Signaling Peptides and ProteinsMembrane ProteinsNerve Tissue ProteinsRabphilin-3AReceptors, N-Methyl-D-AspartateVesicular Transport Proteins

Identifiers

PMID26679993
PMCPMC4703873
OpenAlexW2224134472

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.