Evidence map›Paper›PMID 22837753›Full record

ArticleFrontiers in endocrinology2012

BRET and Time-resolved FRET strategy to study GPCR oligomerization: from cell lines toward native tissues.

Martin Cottet, Orestis Faklaris, Damien Maurel, Pauline Scholler, Etienne Doumazane, Eric Trinquet, Jean-Philippe Pin, Thierry Durroux

Open access · goldAbstract read
In one paragraph

Article in Frontiers in endocrinology, 2012. 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
3.6field-weighted citation impact, top 6% 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, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. The World of GPCR dimers - Mapping dopamine receptor DComputational and structural biotechnology journal · 2023
    Article
  6. Review
  7. Orthogonal Peptide-Templated Labeling Elucidates Lateral ETChembiochem : a European journal of chemical biology · 2022
    Article
  8. Review
  9. Article
  10. Multiple GPCR Functional Assays Based on Resonance Energy Transfer Sensors.Frontiers in cell and developmental biology · 2021
    Review
  11. Article
  12. Striatal Dopamine DFrontiers in pharmacology · 2020
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. FSHR Trans-Activation and Oligomerization.Frontiers in endocrinology · 2018
    Review
  19. Review
  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

8 authors at 4 institutions in 1 country.

Martin CottetInstitut de Génomique Fonctionnelle CNRS, UMR 5203, Montpellier, France.
Orestis Faklaris
Damien Maurel
Pauline Scholler
Etienne Doumazane
Eric Trinquet
Jean-Philippe Pin
Thierry Durroux
Inserm · FRCentre National de la Recherche Scientifique · FRUniversité de Montpellier · FRCisbio (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The concept of oligomerization of G protein-coupled receptor (GPCR) opens new perspectives regarding physiological function regulation. The capacity of one GPCR to modify its binding and coupling properties by interacting with a second one can be at the origin of regulations unsuspected two decades ago. Although the concept is interesting, its validation at a physiological level is challenging and probably explains why receptor oligomerization is still controversial. Demonstrating direct interactions between two proteins is not trivial since few techniques present a spatial resolution allowing this precision. Resonance energy transfer (RET) strategies are actually the most convenient ones. During the last two decades, bioluminescent resonance energy transfer and time-resolved fluorescence resonance energy transfer (TR-FRET) have been widely used since they exhibit high signal-to-noise ratio. Most of the experiments based on GPCR labeling have been performed in cell lines and it has been shown that all GPCRs have the propensity to form homo- or hetero-oligomers. However, whether these data can be extrapolated to GPCRs expressed in native tissues and explain receptor functioning in real life, remains an open question. Native tissues impose different constraints since GPCR sequences cannot be modified. Recently, a fluorescent ligand-based GPCR labeling strategy combined to a TR-FRET approach has been successfully used to prove the existence of GPCR oligomerization in native tissues. Although the RET-based strategies are generally quite simple to implement, precautions have to be taken before concluding to the absence or the existence of specific interactions between receptors. For example, one should exclude the possibility of collision of receptors diffusing throughout the membrane leading to a specific FRET signal. The advantages and the limits of different approaches will be reviewed and the consequent perspectives discussed.

Indexed as

BRETfluorescencefluorescent ligandFRETG protein-coupled receptoroligomertime-resolved FRET

Identifiers

PMID22837753
PMCPMC3401989
OpenAlexW2082357358

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.