ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2011
Allosteric interactions across native adenosine-A3 receptor homodimers: quantification using single-cell ligand-binding kinetics.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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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
46 citing papers in PubMed, 84 citations in OpenAlex.
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- Fluorescent ligands: Bringing light to emerging GPCR paradigms.British journal of pharmacology · 2020Review
- Chemical Probes for the Adenosine Receptors.Pharmaceuticals (Basel, Switzerland) · 2019Review
- Ligand Binding Dynamics for Pre-dimerised G Protein-Coupled Receptor Homodimers: Linear Models and Analytical Solutions.Bulletin of mathematical biology · 2019Article
- Complex Formation between VEGFR2 and the βCell chemical biology · 2019Article
- Binding kinetics of ligands acting at GPCRs.Molecular and cellular endocrinology · 2019Review
- The Endocannabinoid System as a Target in Cancer Diseases: Are We There Yet?Frontiers in pharmacology · 2019Review
- Reinterpreting anomalous competitive binding experiments within G protein-coupled receptor homodimers using a dimer receptor model.Pharmacological research · 2019Article
- New paradigms in adenosine receptor pharmacology: allostery, oligomerization and biased agonism.British journal of pharmacology · 2018Review
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- Spatial Intensity Distribution Analysis: Studies of G Protein-Coupled Receptor Oligomerisation.Trends in pharmacological sciences · 2018Review
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A growing awareness indicates that many G-protein-coupled receptors (GPCRs) exist as homodimers, but the extent of the cooperativity across the dimer interface has been largely unexplored. Here, measurement of the dissociation kinetics of a fluorescent agonist (ABA-X-BY630) from the human A(1) or A(3) adenosine receptors expressed in CHO-K1 cells has provided evidence for highly cooperative interactions between protomers of the A(3)-receptor dimer in single living cells. In the absence of competitive ligands, the dissociation rate constants of ABA-X-BY630 from A(1) and A(3) receptors were 1.45 ± 0.05 and 0.57 ± 0.07 min(-1), respectively. At the A(3) receptor, this could be markedly increased by both orthosteric agonists and antagonists [15-, 9-, and 19-fold for xanthine amine congener (XAC), 5'-(N-ethyl carboxamido)adenosine (NECA), and adenosine, respectively] and reduced by coexpression of a nonbinding (N250A) A(3)-receptor mutant. The changes in ABA-X-BY630 dissociation were much lower at the A(1) receptor (1.5-, 1.4-, and 1.5-fold). Analysis of the pEC(50) values of XAC, NECA, and adenosine for the ABA-X-BY630-occupied A(3)-receptor dimer yielded values of 6.0 ± 0.1, 5.9 ± 0.1, and 5.2 ± 0.1, respectively. This study provides new insight into the spatial and temporal specificity of drug action that can be provided by allosteric modulation across a GPCR homodimeric interface.
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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.