ArticleProceedings of the National Academy of Sciences of the United States of America2013
Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 229 papers.
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Who cites it
229 citing papers in PubMed, 436 citations in OpenAlex.
- Atomic, structural and molecular insights into GPCR ligand binding and signalling.Nature reviews. Molecular cell biology · 2026Review
- G protein diffusion states reveal receptor binding dynamics at single-molecule scale.Cell chemical biology · 2026Article
- Characterizing cellular receptor dynamics in live fluorescence imaging using stochastic modeling and machine learning.iScience · 2026Article
- Characterising C-X-C Chemokine Receptor 4 Dynamics in the Cell Membrane Using Fluorescence Fluctuation Spectroscopy.Biomolecules · 2026Article
- Graph neural network modeling of receptor interaction kinetics from single-molecule imaging data.bioRxiv : the preprint server for biology · 2026Article
- Biomolecular assemblies through weak noncovalent interactions: Higher-order transient structures and their condensate phase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- HIV-1 envelope glycoprotein modulates CXCR4 clustering and dynamics on the T cell membrane.eLife · 2026Article
- Receptor homodimerization significantly prolongs the lifetime of ligand-induced cross-linking of CLEC-2 but not GPVI.Blood vessels, thrombosis & hemostasis · 2026Article
- Spatiotemporal Organization of PTK7 Diffusion on Cell Surface Facilitates Tumor Invasion and Migration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.Nature communications · 2026Article
- Unraveling allosteric signaling of G protein-coupled receptors (GPCRs) by single-molecule fluorescence.Biophysical reviews · 2026Review
- Differential conservation analysis identifies residues defining constitutive internalization in beta-adrenergic receptors.iScience · 2026Article
- Functional and structural basis of a negative allostery within GABANature communications · 2026Article
- Allosteric activation of the glutamate receptor mGlu2 by the serotonin receptor 5-HTNature communications · 2026Article
- A general one-step protocol to generate impermeable fluorescent HaloTag substrates for in situ live cell application and super-resolution imaging.Nature communications · 2026Article
- Exploring Biophysics at the Membrane with Single-Molecule TIRF Microscopy.Advances in experimental medicine and biology · 2026Review
- Single-molecule characterization of opioid receptor heterodimers reveals soluble µ-δ dimer blocker peptide alleviates morphine tolerance.Nature communications · 2025Article
- Functional significance of opioid receptor homomers and heteromers.Nature communications · 2025Article
- Single-molecule methods for characterizing receptor dimers reveal metastable opioid receptor homodimers that induce functional modulation.Nature communications · 2025Article
- Cholesterol oxidase treatment impairs CXCR4-mediated T cell migration.Cell communication and signaling : CCS · 2025Article
169 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein-coupled receptors (GPCRs) constitute the largest family of receptors and major pharmacological targets. Whereas many GPCRs have been shown to form di-/oligomers, the size and stability of such complexes under physiological conditions are largely unknown. Here, we used direct receptor labeling with SNAP-tags and total internal reflection fluorescence microscopy to dynamically monitor single receptors on intact cells and thus compare the spatial arrangement, mobility, and supramolecular organization of three prototypical GPCRs: the β(1)-adrenergic receptor (β(1)AR), the β(2)-adrenergic receptor (β(2)AR), and the γ-aminobutyric acid (GABA(B)) receptor. These GPCRs showed very different degrees of di-/oligomerization, lowest for β(1)ARs (monomers/dimers) and highest for GABA(B) receptors (prevalently dimers/tetramers of heterodimers). The size of receptor complexes increased with receptor density as a result of transient receptor-receptor interactions. Whereas β(1)-/β(2)ARs were apparently freely diffusing on the cell surface, GABA(B) receptors were prevalently organized into ordered arrays, via interaction with the actin cytoskeleton. Agonist stimulation did not alter receptor di-/oligomerization, but increased the mobility of GABA(B) receptor complexes. These data provide a spatiotemporal characterization of β(1)-/β(2)ARs and GABA(B) receptors at single-molecule resolution. The results suggest that GPCRs are present on the cell surface in a dynamic equilibrium, with constant formation and dissociation of new receptor complexes that can be targeted, in a ligand-regulated manner, to different cell-surface microdomains.
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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.