ArticleBiophysical journal2015
Referenced Single-Molecule Measurements Differentiate between GPCR Oligomerization States.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- Synthetic FLS2 receptor oligomer boosts plant innate immunity.Science advances · 2026Article
- Quantification of absolute labeling efficiency at the single-protein level.Nature methods · 2024Article
- Real-time imaging of axonal membrane protein life cycles.Nature protocols · 2024Review
- ProDOL: a general method to determine the degree of labeling for staining optimization and molecular counting.Nature methods · 2024Article
- Diffusion and Oligomerization States of the Muscarinic MThe journal of physical chemistry. B · 2024Article
- Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells.Nature protocols · 2021Article
- Constraints on GPCR Heterodimerization Revealed by the Type-4 Induced-Association BRET Assay.Biophysical journal · 2019Article
- Exocyst dynamics during vesicle tethering and fusion.Nature communications · 2018Article
- The Class-A GPCR Dopamine D2 Receptor Forms Transient Dimers Stabilized by Agonists: Detection by Single-Molecule Tracking.Cell biochemistry and biophysics · 2018Article
- Article
- Receptor Quaternary Organization Explains G Protein-Coupled Receptor Family Structure.Cell reports · 2017Article
- Spatial intensity distribution analysis quantifies the extent and regulation of homodimerization of the secretin receptor.The Biochemical journal · 2017Article
- Attenuation of chemokine receptor function and surface expression as an immunomodulatory strategy employed by human cytomegalovirus is linked to vGPCR US28.Cell communication and signaling : CCS · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The extent to which Rhodopsin family G-protein-coupled receptors (GPCRs) form invariant oligomers is contentious. Recent single-molecule fluorescence imaging studies mostly argue against the existence of constitutive receptor dimers and instead suggest that GPCRs only dimerize transiently, if at all. However, whether or not even transient dimers exist is not always clear due to difficulties in unambiguously distinguishing genuine interactions from chance colocalizations, particularly with respect to short-lived events. Previous single-molecule studies have depended critically on calculations of chance colocalization rates and/or comparison with unfixed control proteins whose diffusional behavior may or may not differ from that of the test receptor. Here, we describe a single-molecule imaging assay that 1) utilizes comparisons with well-characterized control proteins, i.e., the monomer CD86 and the homodimer CD28, and 2) relies on cell fixation to limit artifacts arising from differences in the distribution and diffusion of test proteins versus these controls. The improved assay reliably reports the stoichiometry of the Glutamate-family GPCR dimer, γ-amino butyric acid receptor b2, whereas two Rhodopsin-family GPCRs, β2-adrenergic receptor and mCannR2, exhibit colocalization levels comparable to those of CD86 monomers, strengthening the case against invariant GPCR oligomerization.
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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.