Evidence map›Paper›PMID 27313205›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structural rearrangement of the intracellular domains during AMPA receptor activation.

Linda G Zachariassen, Ljudmila Katchan, Anna G Jensen, Darryl S Pickering, Andrew J R Plested, Anders S Kristensen

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Frontiers in cellular neuroscience · 2026
    Review
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  3. Review
  4. Article
  5. Review
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  7. Article
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  9. Article
  10. Review
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  12. Review
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  14. Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Relative positioning of Kv11.1 (hERG) KScientific reports · 2018
    Article
  18. Review
  19. Properties of TriheteromericMolecular pharmacology · 2018
    Article
  20. Article
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

6 authors.

Linda G ZachariassenDepartment of Drug Design & Pharmacology, University of Copenhagen, DK-2100 Copenhagen, Denmark;
Ljudmila KatchanMolecular Neuroscience and Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany; Cluster of Excellence NeuroCure, Charité Universitätsmedizin, 10117 Berlin, Germany.
Anna G JensenDepartment of Drug Design & Pharmacology, University of Copenhagen, DK-2100 Copenhagen, Denmark;
Darryl S PickeringDepartment of Drug Design & Pharmacology, University of Copenhagen, DK-2100 Copenhagen, Denmark;
Andrew J R PlestedMolecular Neuroscience and Biophysics, Leibniz-Institut für Molekulare Pharmakologie, 13125 Berlin, Germany; Cluster of Excellence NeuroCure, Charité Universitätsmedizin, 10117 Berlin, Germany plested@fmp-berlin.de ask@sund.ku.dk.
Anders S KristensenDepartment of Drug Design & Pharmacology, University of Copenhagen, DK-2100 Copenhagen, Denmark; plested@fmp-berlin.de ask@sund.ku.dk.ORCID 0000-0001-8955-6790

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) are ligand-gated ion channels that mediate the majority of fast excitatory neurotransmission in the central nervous system. Despite recent advances in structural studies of AMPARs, information about the specific conformational changes that underlie receptor function is lacking. Here, we used single and dual insertion of GFP variants at various positions in AMPAR subunits to enable measurements of conformational changes using fluorescence resonance energy transfer (FRET) in live cells. We produced dual CFP/YFP-tagged GluA2 subunit constructs that had normal activity and displayed intrareceptor FRET. We used fluorescence lifetime imaging microscopy (FLIM) in live HEK293 cells to determine distinct steady-state FRET efficiencies in the presence of different ligands, suggesting a dynamic picture of the resting state. Patch-clamp fluorometry of the double- and single-insert constructs showed that both the intracellular C-terminal domain (CTD) and the loop region between the M1 and M2 helices move during activation and the CTD is detached from the membrane. Our time-resolved measurements revealed unexpectedly complex fluorescence changes within these intracellular domains, providing clues as to how posttranslational modifications and receptor function interact.

Indexed as

AnimalsFemaleFluorescence Resonance Energy TransferHEK293 CellsHumansPatch-Clamp TechniquesReceptors, AMPAXenopus laevisglutamate receptor ionotropic, AMPA 2Receptors, AMPAAMPAelectrophysiologyFRETglutamate

Identifiers

PMID27313205
PMCPMC4941491

What OpenQuestion holds

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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.