ArticleThe Journal of biological chemistry2010
Interactions between intracellular domains as key determinants of the quaternary structure and function of receptor heteromers.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 111 citations in OpenAlex.
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- Conformational Restriction of Designer Drugs Reveals Subtype-Selective and Biased CBJournal of medicinal chemistry · 2025Article
- The effect of peripheral dopamine on fracture healing: an experimental study in a rat model.Journal of orthopaedic surgery and research · 2025Article
- Design of Small Non-Peptidic Ligands That Alter Heteromerization between Cannabinoid CBJournal of medicinal chemistry · 2025Article
- Allosteric modulation of gonadotropin receptors.Frontiers in endocrinology · 2023Review
- Modulating brain integrative actions as a new perspective on pharmacological approaches to neuropsychiatric diseases.Frontiers in endocrinology · 2022Review
- Modulation of adenosine A2a receptor oligomerization by receptor activation and PIPStructure (London, England : 1993) · 2021Article
- Carnitine palmitoyltransferase 1C negatively regulates the endocannabinoid hydrolase ABHD6 in mice, depending on nutritional status.British journal of pharmacology · 2021Article
- Structure and function of adenosine receptor heteromers.Cellular and molecular life sciences : CMLS · 2021Review
- Immunomodulatory Effects of Dopamine in Inflammatory Diseases.Frontiers in immunology · 2021Review
- Review
- Adenosine AInternational journal of molecular sciences · 2020Article
- Adreno-melatonin receptor complexes control ion homeostasis and intraocular pressure - their disruption contributes to hypertensive glaucoma.British journal of pharmacology · 2020Article
- Article
- Experimental and computational analysis of biased agonism on full-length and a C-terminally truncated adenosine AComputational and structural biotechnology journal · 2020Article
- Functional and Neuroprotective Role of Striatal Adenosine AJournal of caffeine and adenosine research · 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
- Singular Location and Signaling Profile of Adenosine ANeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
G protein-coupled receptor (GPCR) heteromers are macromolecular complexes with unique functional properties different from those of its individual protomers. Little is known about what determines the quaternary structure of GPCR heteromers resulting in their unique functional properties. In this study, using resonance energy transfer techniques in experiments with mutated receptors, we provide for the first time clear evidence for a key role of intracellular domains in the determination of the quaternary structure of GPCR heteromers between adenosine A(2A), cannabinoid CB(1), and dopamine D(2) receptors. In these interactions, arginine-rich epitopes form salt bridges with phosphorylated serine or threonine residues from CK1/2 consensus sites. Each receptor (A(2A), CB(1), and D(2)) was found to include two evolutionarily conserved intracellular domains to establish selective electrostatic interactions with intracellular domains of the other two receptors, indicating that these particular electrostatic interactions constitute a general mechanism for receptor heteromerization. Mutation experiments indicated that the interactions of the intracellular domains of the CB(1) receptor with A(2A) and D(2) receptors are fundamental for the correct formation of the quaternary structure needed for the function (MAPK signaling) of the A(2A)-CB(1)-D(2) receptor heteromers. Analysis of MAPK signaling in striatal slices of CB(1) receptor KO mice and wild-type littermates supported the existence of A(1)-CB(1)-D(2) receptor heteromer in the brain. These findings allowed us to propose the first molecular model of the quaternary structure of a receptor heteromultimer.
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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.