Evidence map›Paper›PMID 19763081›Full record

ArticleThe EMBO journal2009

Ligand-regulated oligomerization of beta(2)-adrenoceptors in a model lipid bilayer.

Juan José Fung, Xavier Deupi, Leonardo Pardo, Xiao Jie Yao, Gisselle A Velez-Ruiz, Brian T Devree, Roger K Sunahara, Brian K Kobilka

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

85 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
  2. Construction of αJournal of separation science · 2026
    Article
  3. Article
  4. Article
  5. A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Interrogating surfaceChemical science · 2020
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Juan José FungDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Xavier Deupi
Leonardo Pardo
Xiao Jie Yao
Gisselle A Velez-Ruiz
Brian T Devree
Roger K Sunahara
Brian K Kobilka
Stanford University · USUniversity of Michigan–Ann Arbor · USUniversitat Autònoma de Barcelona · ES

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
THE MECHANISM OF BETA2 ADRENOCEPTOR ACTIVATIONR01NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 1990 to 2021
$6.7M
Beta2 Adrenoceptor Structure and Mechanism of ActivationR37NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 2005 to 2011
$3.9M
Structure and mechanism of beta2-adrenergic receptorR01GM068603 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUNAHARA, ROGER K · 2003 to 2008
$1.6M
NIGMS NIH HHS GM007276NIGMS NIH HHS R01 GM068603NIGMS NIH HHS R01-GM068603NIGMS NIH HHS T32 GM007276NIGMS NIH HHS T32 GM007315NINDS NIH HHS NS28471NINDS NIH HHS R01 NS028471NINDS NIH HHS R37 NS028471
6 · The paper itself

Abstract

The beta(2)-adrenoceptor (beta(2)AR) was one of the first Family A G protein-coupled receptors (GPCRs) shown to form oligomers in cellular membranes, yet we still know little about the number and arrangement of protomers in oligomers, the influence of ligands on the organization or stability of oligomers, or the requirement for other proteins to promote oligomerization. We used fluorescence resonance energy transfer (FRET) to characterize the oligomerization of purified beta(2)AR site-specifically labelled at three different positions with fluorophores and reconstituted into a model lipid bilayer. Our results suggest that the beta(2)AR is predominantly tetrameric following reconstitution into phospholipid vesicles. Agonists and antagonists have little effect on the relative orientation of protomers in oligomeric complexes. In contrast, binding of inverse agonists leads to significant increases in FRET efficiencies for most labelling pairs, suggesting that this class of ligand promotes tighter packing of protomers and/or the formation of more complex oligomers by reducing conformational fluctuations in individual protomers. The results provide new structural insights into beta(2)AR oligomerization and suggest a possible mechanism for the functional effects of inverse agonists.

Indexed as

CysteineFluorescence Resonance Energy TransferGTP-Binding ProteinsHumansLigandsLipid BilayersLiposomesModels, MolecularPoint MutationProtein BindingProtein MultimerizationReceptors, Adrenergic, beta-2CysteineGTP-Binding ProteinsLigandsLipid BilayersLiposomesReceptors, Adrenergic, beta-2

Identifiers

PMID19763081
PMCPMC2748299
OpenAlexW1965064544

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.