Evidence map›Paper›PMID 19144831›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009

Agonist occupancy is essential for forward trafficking of AMPA receptors.

Sarah K Coleman, Tommi Möykkynen, Annukka Jouppila, Susanna Koskelainen, Claudio Rivera, Esa R Korpi, Kari Keinänen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

  1. Distinct Regulation of Early Trafficking of the NMDA Receptors by the Ligand-Binding Domains of the GluN1 and GluN2A Subunits.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
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  16. Cornichons modify channel properties of recombinant and glial AMPA receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
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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

7 authors at 1 institution in 1 country.

Sarah K ColemanDepartment of Biological and Environmental Sciences, Division of Biochemistry, Viikki Biocenter, University of Helsinki, Helsinki, Finland.
Tommi Möykkynen
Annukka Jouppila
Susanna Koskelainen
Claudio Rivera
Esa R Korpi
Kari Keinänen
University of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulated trafficking of AMPA receptors to cell surface and to synapses is an important determinant of neuronal excitability. In the present study, we have addressed the role of agonist binding and desensitization in the early trafficking of glutamate receptor-D (GluR-D) AMPA receptors. Analysis of point-mutated GluR-D receptors, via electrophysiology and immunofluorescence, revealed that agonist-binding activity is essential for efficient delivery to cell surface in transfected cell lines and in neurons. Cotransfection with stargazin could fully rescue the surface expression of nonbinding mutant receptors in cell lines, indicating that stargazin is able to interact with and promote exit of AMPA receptors from endoplasmic reticulum (ER) independently of agonist binding. Secretion of separately expressed ligand-binding domain constructs showed a similar dependency of agonist binding to that observed with full-length GluR-D, supporting the idea that glutamate-induced closure of the binding site cleft is registered by ER quality control as a necessary priming step for transport competence. In contrast to agonist binding, the ability of the receptor to undergo desensitization had only a minor influence on trafficking. Our results are consistent with the hypothesis that AMPA receptors are synthesized as intrinsically unstable molecules, which require glutamate binding for structural stability and for transport-competence.

Indexed as

AnimalsBinding SitesBiotinylationCell Line, TransformedChlorocebus aethiopsExcitatory Amino Acid AgonistsExcitatory Amino Acid AntagonistsGreen Fluorescent ProteinsHumansMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane PotentialsModels, MolecularPatch-Clamp TechniquesPoint MutationProtein BindingProtein Structure, Tertiary2,3-dioxo-6-nitro-7-sulfamoylbenzo(f)quinoxalineExcitatory Amino Acid AgonistsExcitatory Amino Acid AntagonistsGreen Fluorescent ProteinsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseQuinoxalinesReceptors, AMPA

Identifiers

PMID19144831
PMCPMC6664942
OpenAlexW2075663998

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.