Evidence map›Paper›PMID 20837486›Full record

ArticleThe Journal of biological chemistry2010

Ligand-binding domain determines endoplasmic reticulum exit of AMPA receptors.

Sarah K Coleman, Tommi Möykkynen, Sami Hinkkuri, Lauri Vaahtera, Esa R Korpi, Olli T Pentikäinen, Kari Keinänen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
0.8field-weighted citation impact, top 32% 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, 31 citations in OpenAlex.

  1. Paradoxical Expression of Ionotropic Glutamate Receptors in Leucocytes.Clinical reviews in allergy & immunology · 2026
    Article
  2. Frontiers in cellular neuroscience · 2026
    Review
  3. Article
  4. 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
    Article
  5. Article
  6. Review
  7. Mechanisms of CPT1C-Dependent AMPAR Trafficking Enhancement.Frontiers in molecular neuroscience · 2018
    Article
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  15. Review
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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 3 institutions in 1 country.

Sarah K ColemanDepartment of Biosciences, Division of Biochemistry, Viikki Biocenter, University of Helsinki, FI-00014 University of Helsinki, Finland.
Tommi Möykkynen
Sami Hinkkuri
Lauri Vaahtera
Esa R Korpi
Olli T Pentikäinen
Kari Keinänen
University of Helsinki · FIBiocenter Finland · FIUniversity of Jyväskylä · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMPA receptors (AMPARs) are tetrameric ion channels that mediate rapid glutamate signaling in neurons and many non-neuronal cell types. Endoplasmic reticulum (ER) quality control mechanisms permit only correctly folded functional receptors to be delivered to the cell surface. We analyzed the biosynthetic maturation and transport of all 12 GluA1-4 subunit splice variants as homomeric receptors and observed robust isoform-dependent differences in ER exit competence and surface expression. In contrast to inefficient ER exit of both GluA3 splice forms and the flop variants of GluA1 and GluA4, prominent plasma membrane expression was observed for the other AMPAR isoforms. Surprisingly, deletion of the entire N-terminal domain did not alter the transport phenotype, nor did the different cytosolic C-terminal tail splice variants. Detailed analysis of mutant receptors led to the identification of distinct residues in the ligand-binding domain as primary determinants for isoform-specific maturation. Considered together with the essential role of bound agonist, our findings reveal the ligand-binding domain as the critical quality control target in AMPAR biogenesis.

Indexed as

Protein Structure, TertiaryAlternative SplicingAmino Acid SequenceAnimalsBinding SitesCell MembraneChlorocebus aethiopsCOS CellsEndoplasmic ReticulumHEK293 CellsHumansImmunoblottingLigandsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataLigandsProtein IsoformsProtein SubunitsReceptors, AMPA

Identifiers

PMID20837486
PMCPMC2975225
OpenAlexW2078300126

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.