ArticleCell reports2017
Receptor Quaternary Organization Explains G Protein-Coupled Receptor Family Structure.
Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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.
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.
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Who cites it
26 citing papers in PubMed.
- Cellular context and ligand class shape CXCR4-CCR5 heteromerization in live cells.Research square · 2026Article
- Allosteric activation of the glutamate receptor mGlu2 by the serotonin receptor 5-HTNature communications · 2026Article
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- Structural insights into Wnt/β-catenin signaling regulation by LGR4, R-spondin, and ZNRF3.Nature communications · 2025Article
- Structural insights into the LGR4-RSPO2-ZNRF3 complexes regulating WNT/β-catenin signaling.Nature communications · 2025Article
- LGR4 and LGR5 form distinct homodimers that only LGR4 complexes with RNF43/ZNRF3 to provide high affinity binding of R-spondin ligands.Scientific reports · 2023Article
- Differential effects of mutations of POPDC proteins on heteromeric interaction and membrane trafficking.Acta neuropathologica communications · 2023Article
- Computationally designed GPCR quaternary structures bias signaling pathway activation.Nature communications · 2022Article
- Single-molecule counting applied to the study of GPCR oligomerization.Biophysical journal · 2022Review
- Article
- Evolutionary Constraint on Visual and Nonvisual Mammalian Opsins.Journal of biological rhythms · 2021Article
- Determination of G-protein-coupled receptor oligomerization by molecular brightness analyses in single cells.Nature protocols · 2021Article
- An expectation-maximization approach to quantifying protein stoichiometry with single-molecule imaging.Bioinformatics advances · 2021Article
- Purinergic GPCR transmembrane residues involved in ligand recognition and dimerization.Methods in cell biology · 2021Review
- Unlike LGR4, LGR5 potentiates Wnt-β-catenin signaling without sequestering E3 ligases.Science signaling · 2020Article
- Interclass GPCR heteromerization affects localization and trafficking.Science signaling · 2020Article
- New Advances in Targeting the Resolution of Inflammation: Implications for Specialized Pro-Resolving Mediator GPCR Drug Discovery.ACS pharmacology & translational science · 2020Review
- Combinatorial allosteric modulation of agonist response in a self-interacting G-protein coupled receptor.Communications biology · 2020Article
- Luminescence- and Fluorescence-Based Complementation Assays to Screen for GPCR Oligomerization: Current State of the Art.International journal of molecular sciences · 2019Review
- Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology.Molecules (Basel, Switzerland) · 2019Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The organization of Rhodopsin-family G protein-coupled receptors (GPCRs) at the cell surface is controversial. Support both for and against the existence of dimers has been obtained in studies of mostly individual receptors. Here, we use a large-scale comparative study to examine the stoichiometric signatures of 60 receptors expressed by a single human cell line. Using bioluminescence resonance energy transfer- and single-molecule microscopy-based assays, we found that a relatively small fraction of Rhodopsin-family GPCRs behaved as dimers and that these receptors otherwise appear to be monomeric. Overall, the analysis predicted that fewer than 20% of ∼700 Rhodopsin-family receptors form dimers. The clustered distribution of the dimers in our sample and a striking correlation between receptor organization and GPCR family size that we also uncover each suggest that receptor stoichiometry might have profoundly influenced GPCR expansion and diversification.
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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.