Evidence map›Paper›PMID 28424368›Full record

ArticleThe Biochemical journal2017

Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.

Richard J Ward, John D Pediani, Kaleeckal G Harikumar, Laurence J Miller, Graeme Milligan

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Intensity-Based Estimation of Monomeric Brightness for Fluorescent Proteins.International journal of molecular sciences · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. The MProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. GPCR homo-oligomerization.Current opinion in cell biology · 2019
    Review
  16. Muscarinic receptor oligomerization.Neuropharmacology · 2018
    Review
  17. Review
  18. 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

5 authors at 2 institutions in 2 countries.

Richard J WardCentre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Wolfson Link Building 253, Glasgow G12 8QQ, U.K.
John D PedianiCentre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Wolfson Link Building 253, Glasgow G12 8QQ, U.K.
Kaleeckal G HarikumarDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, 13400 East Shea Blvd, Scottsdale, AZ 85259, U.S.A.
Laurence J MillerDepartment of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, 13400 East Shea Blvd, Scottsdale, AZ 85259, U.S.A.
Graeme MilliganCentre for Translational Pharmacology, Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, Wolfson Link Building 253, Glasgow G12 8QQ, U.K. graeme.milligan@glasgow.ac.uk.
University of Glasgow · GBMayo Clinic in Arizona · US

Funding

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

Abstract

Previous studies have indicated that the G-protein-coupled secretin receptor is present as a homodimer, organized through symmetrical contacts in transmembrane domain IV, and that receptor dimerization is critical for high-potency signalling by secretin. However, whether all of the receptor exists in the dimeric form or if this is regulated is unclear. We used measures of quantal brightness of the secretin receptor tagged with monomeric enhanced green fluorescent protein (mEGFP) and spatial intensity distribution analysis to assess this. Calibration using cells expressing plasma membrane-anchored forms of mEGFP initially allowed us to demonstrate that the epidermal growth factor receptor is predominantly monomeric in the absence of ligand and while wild-type receptor was rapidly converted into a dimeric form by ligand, a mutated form of this receptor remained monomeric. Equivalent studies showed that, at moderate expression levels, the secretin receptor exists as a mixture of monomeric and dimeric forms, with little evidence of higher-order complexity. However, sodium butyrate-induced up-regulation of the receptor resulted in a shift from monomeric towards oligomeric organization. In contrast, a form of the secretin receptor containing a pair of mutations on the lipid-facing side of transmembrane domain IV was almost entirely monomeric. Down-regulation of the secretin receptor-interacting G-protein Gα

Indexed as

AnimalsCHO CellsCricetinaeCricetulusGreen Fluorescent ProteinsProtein MultimerizationReceptors, Gastrointestinal HormoneReceptors, G-Protein-Coupledenhanced green fluorescent proteinGreen Fluorescent ProteinsReceptors, Gastrointestinal HormoneReceptors, G-Protein-Coupledsecretin receptorG-protein-coupled receptorsquaternary structurespatial intensity distribution analysis

Identifiers

PMID28424368
PMCPMC5442643
OpenAlexW2606990326

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.