ArticleMolecular pharmacology2013
Fluorescence correlation spectroscopy analysis of serotonin, adrenergic, muscarinic, and dopamine receptor dimerization: the oligomer number puzzle.
Article in Molecular pharmacology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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.
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.
Who cites it
45 citing papers in PubMed, 124 citations in OpenAlex.
- Measuring Membrane Protein Dynamics in Plant Roots Using Fluorescence Correlation Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Neurochemical profiling in urine: Multiplexed detection of dopamine and serotonin using ML-integrated laser-induced graphene biosensors.Biosensors & bioelectronics · 2025Article
- Single-molecule localization microscopy as a tool to quantify di/oligomerization of receptor tyrosine kinases and G protein-coupled receptors.Molecular pharmacology · 2025Review
- Article
- Intercellular Communication in the Central Nervous System as Deduced by Chemical Neuroanatomy and Quantitative Analysis of Images: Impact on Neuropharmacology.International journal of molecular sciences · 2022Review
- Combined Free-Energy Calculation and Machine Learning Methods for Understanding Ligand Unbinding Kinetics.Journal of chemical theory and computation · 2022Article
- G protein-coupled receptor-effector macromolecular membrane assemblies (GEMMAs).Pharmacology & therapeutics · 2022Review
- Heterobivalent Ligand for the Adenosine AJournal of medicinal chemistry · 2022Article
- Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells.Nature protocols · 2021Article
- βFrontiers in cardiovascular medicine · 2021Article
- International Union of Basic and Clinical Pharmacology. CX. Classification of Receptors for 5-hydroxytryptamine; Pharmacology and Function.Pharmacological reviews · 2021Review
- Oligomerization of G protein-coupled receptors: Still doubted?Progress in molecular biology and translational science · 2020Review
- Quantifying the Oligomeric State of hZIP4 on the Surface of Cells.Biochemistry · 2019Article
- GPCR homo-oligomerization.Current opinion in cell biology · 2019Review
- The Endocannabinoid System as a Target in Cancer Diseases: Are We There Yet?Frontiers in pharmacology · 2019Review
- Receptor-Receptor Interactions as a Widespread Phenomenon: Novel Targets for Drug Development?Frontiers in endocrinology · 2019Review
- Global analysis of protein homomerization inGenome research · 2019Article
- Reinterpreting anomalous competitive binding experiments within G protein-coupled receptor homodimers using a dimer receptor model.Pharmacological research · 2019Article
- Ligand-Induced Coupling between Oligomers of the MBiophysical journal · 2018Article
- Muscarinic receptor oligomerization.Neuropharmacology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The issue of G protein-coupled receptor (GPCR) oligomer status has not been resolved. Although many studies have provided evidence in favor of receptor-receptor interactions, there is no consensus as to the exact oligomer size of class A GPCRs. Previous studies have reported monomers, dimers, tetramers, and higher-order oligomers. In the present study, this issue was examined using fluorescence correlation spectroscopy (FCS) with photon counting histogram (PCH) analysis, a sensitive method for monitoring diffusion and oligomer size of plasma membrane proteins. Six different class A GPCRs were selected from the serotonin (5-HT2A), adrenergic (α1b-AR and β2-AR), muscarinic (M1 and M2), and dopamine (D1) receptor families. Each GPCR was C-terminally labeled with green fluorescent protein (GFP) or yellow fluorescent protein (YFP) and expressed in human embryonic kidney 293 cells. FCS provided plasma membrane diffusion coefficients on the order of 7.5 × 10(-9) cm(2)/s. PCH molecular brightness analysis was used to determine the GPCR oligomer size. Known monomeric (CD-86) and dimeric (CD-28) receptors with GFP and YFP tags were used as controls to determine the molecular brightness of monomers and dimers. PCH analysis of fluorescence-tagged GPCRs revealed molecular brightness values that were twice the monomeric controls and similar to the dimeric controls. Reduced χ(2) analyses of the PCH data best fit a model for a homogeneous population of homodimers, without tetramers or higher-order oligomers. The homodimer configuration was unaltered by agonist treatment and was stable over a 10-fold range of receptor expression level. The results of this study demonstrate that biogenic amine receptors freely diffusing within the plasma membrane are predominantly homodimers.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.