Evidence map›Paper›PMID 22815494›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2012

Cornichons modify channel properties of recombinant and glial AMPA receptors.

Ian D Coombs, David Soto, Marzieh Zonouzi, Massimiliano Renzi, Chris Shelley, Mark Farrant, Stuart G Cull-Candy

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed, 2 pooled it
3.7field-weighted citation impact, top 6% 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

67 citing papers in PubMed, 2 syntheses or guidelines pooled it, 108 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  5. Review
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  9. Trafficking of the human NaProtein science : a publication of the Protein Society · 2026
    Article
  10. From Atoms to Neuronal Spikes: A Multiscale Simulation Framework.Journal of chemical theory and computation · 2026
    Review
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  13. From Atoms to Neuronal Spikes: A Multi-Scale Simulation Framework.bioRxiv : the preprint server for biology · 2025
    Article
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7 more citing papers are in PubMed but not listed here.

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 3 countries.

Ian D CoombsDepartment of Neuroscience, Physiology and Pharmacology, University College London, London WC1E 6BT, United Kingdom.
David Soto
Marzieh Zonouzi
Massimiliano Renzi
Chris Shelley
Mark Farrant
Stuart G Cull-Candy
UCL Australia · AUInstitut d'Investigació Biomédica de Bellvitge · ESUniversity College London · GB

Funding

Medical Research Council MR/J002976/1Wellcome Trust 086185
6 · The paper itself

Abstract

Ionotropic glutamate receptors, which underlie a majority of excitatory synaptic transmission in the CNS, associate with transmembrane proteins that modify their intracellular trafficking and channel gating. Significant advances have been made in our understanding of AMPA-type glutamate receptor (AMPAR) regulation by transmembrane AMPAR regulatory proteins. Less is known about the functional influence of cornichons-unrelated AMPAR-interacting proteins, identified by proteomic analysis. Here we confirm that cornichon homologs 2 and 3 (CNIH-2 and CNIH-3), but not CNIH-1, slow the deactivation and desensitization of both GluA2-containing calcium-impermeable and GluA2-lacking calcium-permeable (CP) AMPARs expressed in tsA201 cells. CNIH-2 and -3 also enhanced the glutamate sensitivity, single-channel conductance, and calcium permeability of CP-AMPARs while decreasing their block by intracellular polyamines. We examined the potential effects of CNIHs on native AMPARs by recording from rat optic nerve oligodendrocyte precursor cells (OPCs), known to express a significant population of CP-AMPARs. These glial cells exhibited surface labeling with an anti-CNIH-2/3 antibody. Two features of their AMPAR-mediated currents-the relative efficacy of the partial agonist kainate (I(KA)/I(Glu) ratio 0.4) and a greater than fivefold potentiation of kainate responses by cyclothiazide-suggest AMPAR association with CNIHs. Additionally, overexpression of CNIH-3 in OPCs markedly slowed AMPAR desensitization. Together, our experiments support the view that CNIHs are capable of altering key properties of AMPARs and suggest that they may do so in glia.

Indexed as

AnimalsCalciumCell LineCells, CulturedEgg ProteinsExcitatory Amino Acid AgonistsFemaleGlutamic AcidHumansIon Channel GatingKainic AcidMaleMembrane ProteinsNeurogliaNeuronsOptic NerveCalciumCNIH1 protein, humanEgg ProteinsExcitatory Amino Acid AgonistsGlutamic AcidKainic AcidMembrane ProteinsReceptors, AMPA

Identifiers

PMID22815494
PMCPMC3428874
OpenAlexW1972391943

What OpenQuestion holds

Textmetadata
LicenceTDM
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.