ArticleScientific reports2015
BRET evidence that β2 adrenergic receptors do not oligomerize in cells.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 54 citations in OpenAlex.
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- The β2-adrenergic receptor associates with CXCR4 multimers in human cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- G protein-coupled estrogen receptor (GPER)/GPR30 forms a complex with the βArchives of biochemistry and biophysics · 2024Article
- Optimization of BRET saturation assays for robust and sensitive cytosolic protein-protein interaction studies.Scientific reports · 2022Article
- The MProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Oligomerization of yeast α-factor receptor detected by fluorescent energy transfer between ligands.Biophysical journal · 2021Article
- Molecular insights into mechanisms of GPCR hijacking byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Quantitative Profiling of WNT-3A Binding to All Human Frizzled Paralogues in HEK293 Cells by NanoBiT/BRET Assessments.ACS pharmacology & translational science · 2021Article
- Unusual mode of dimerization of retinitis pigmentosa-associated F220C rhodopsin.Scientific reports · 2021Article
- Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells.Nature protocols · 2021Article
- Interclass GPCR heteromerization affects localization and trafficking.Science signaling · 2020Article
- Using the novel HiBiT tag to label cell surface relaxin receptors for BRET proximity analysis.Pharmacology research & perspectives · 2019Article
- Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology.Molecules (Basel, Switzerland) · 2019Review
- Direct visualization of single-molecule membrane protein interactions in living cells.PLoS biology · 2018Article
- Single Proteoliposome High-Content Analysis Reveals Differences in the Homo-Oligomerization of GPCRs.Biophysical journal · 2018Article
- The Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists: Detection by Single-Molecule Tracking.Cell biochemistry and biophysics · 2018Article
- ER/K linked GPCR-G protein fusions systematically modulate second messenger response in cells.Scientific reports · 2017Article
- In vivo monitoring of the recruitment and activation of AP-1 by Arf1.Scientific reports · 2017Article
- Conformational biosensors reveal allosteric interactions between heterodimeric AT1 angiotensin and prostaglandin F2α receptors.The Journal of biological chemistry · 2017Article
- Understanding the FRET Signatures of Interacting Membrane Proteins.The Journal of biological chemistry · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Bioluminescence resonance energy transfer (BRET) is often used to study association of membrane proteins, and in particular oligomerization of G protein-coupled receptors (GPCRs). Oligomerization of class A GPCRs is controversial, in part because the methods used to study this question are not completely understood. Here we reconsider oligomerization of the class A β2 adrenergic receptor (β2AR), and reevaluate BRET titration as a method to study membrane protein association. Using inducible expression of the energy acceptor at multiple levels of donor expression we find that BRET between β2AR protomers is directly proportional to the density of the acceptor up to ~3,000 acceptors μm(-2), and does not depend on the density of the donor or on the acceptor:donor (A:D) stoichiometry. In contrast, BRET between tightly-associating control proteins does not depend on the density of the acceptor, but does depend on the density of the donor and on the A:D ratio. We also find that the standard frameworks used to interpret BRET titration experiments rely on simplifying assumptions that are frequently invalid. These results suggest that β2ARs do not oligomerize in cells, and demonstrate a reliable method of assessing membrane protein association with BRET.
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