Evidence map›Paper›PMID 25825490›Full record

ArticleThe Journal of biological chemistry2015

Regulation of oligomeric organization of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor observed by spatial intensity distribution analysis.

Richard J Ward, John D Pediani, Antoine G Godin, Graeme Milligan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

35 citing papers in PubMed, 61 citations in OpenAlex.

  1. Intensity-Based Estimation of Monomeric Brightness for Fluorescent Proteins.International journal of molecular sciences · 2025
    Article
  2. Review
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  4. The MProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    Review
  14. Review
  15. Article
  16. Review
  17. GPCR homo-oligomerization.Current opinion in cell biology · 2019
    Review
  18. Article
  19. Article
  20. Review
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

4 authors at 2 institutions in 2 countries.

Richard J WardFrom the Institute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom.
John D PedianiFrom the Institute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom.
Antoine G Godinthe University of Bordeaux, LP2N, UMR 5298, F-33405 Talence, France, and the Institut d'Optique Graduate School and CNRS, LP2N, UMR 5298, F-33405 Talence, France.
Graeme MilliganFrom the Institute of Molecular, Cell and Systems Biology, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom, Graeme.Milligan@glasgow.ac.uk.
University of Glasgow · GBCentre National de la Recherche Scientifique · FR

Funding

Medical Research Council G0900050Medical Research Council MR/L023806/1
6 · The paper itself

Abstract

The questions of whether G protein-coupled receptors exist as monomers, dimers, and/or oligomers and if these species interconvert in a ligand-dependent manner are among the most contentious current issues in biology. When employing spatial intensity distribution analysis to laser scanning confocal microscope images of cells stably expressing either a plasma membrane-associated form of monomeric enhanced green fluorescent protein (eGFP) or a tandem version of this fluorophore, the eGFP tandem was identified as a dimer. Similar studies on cells stably expressing an eGFP-tagged form of the epidermal growth factor receptor demonstrated that, although largely a monomer in the basal state, this receptor rapidly became predominantly dimeric upon the addition of its ligand epidermal growth factor. In cells induced to express an eGFP-tagged form of the serotonin 5-hydroxytryptamine 2C (5-HT2C) receptor, global analysis of construct quantal brightness was consistent with the predominant form of the receptor being dimeric. However, detailed spatial intensity distribution analysis demonstrated the presence of multiple forms ranging from monomers to higher-order oligomers. Furthermore, treatment with chemically distinct 5-HT2C receptor antagonists resulted in a time-dependent change in the quaternary organization to one in which there was a preponderance of receptor monomers. This antagonist-mediated effect was reversible, because washout of the ligand resulted in the regeneration of many of the oligomeric forms of the receptor.

Indexed as

Green Fluorescent ProteinsHEK293 CellsHumansMultiprotein ComplexesProtein MultimerizationProtein Structure, QuaternaryReceptor, Serotonin, 5-HT2CRecombinant Fusion ProteinsSerotonin 5-HT2 Receptor Antagonistsenhanced green fluorescent proteinGreen Fluorescent ProteinsMultiprotein ComplexesReceptor, Serotonin, 5-HT2CRecombinant Fusion ProteinsSerotonin 5-HT2 Receptor Antagonistsepidermal growth factor receptor (EGFR)G protein-coupled receptor (GPCR)serotoninseven-helix receptorsingle-molecule biophysics

Identifiers

PMID25825490
PMCPMC4432300
OpenAlexW1767831672

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.