ArticleBMC biology2016
Quaternary structure of a G-protein-coupled receptor heterotetramer in complex with Gi and Gs.
Article in BMC biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 110 citations in OpenAlex.
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- Modulating brain integrative actions as a new perspective on pharmacological approaches to neuropsychiatric diseases.Frontiers in endocrinology · 2022Review
- Current Adenosinergic Therapies: What Do Cancer Cells Stand to Gain and Lose?International journal of molecular sciences · 2021Review
- Identification of the Ghrelin and Cannabinoid CBInternational journal of molecular sciences · 2021Article
- Homo-oligomerization of the human adenosine AeLife · 2021Article
- Microglial Adenosine Receptors: From Preconditioning to Modulating the M1/M2 Balance in Activated Cells.Cells · 2021Review
- From purines to purinergic signalling: molecular functions and human diseases.Signal transduction and targeted therapy · 2021Review
- Novel Interactions Involving the Mas Receptor Show Potential of the Renin-Angiotensin system in the Regulation of Microglia Activation: Altered Expression in Parkinsonism and Dyskinesia.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021Article
- Structure and function of adenosine receptor heteromers.Cellular and molecular life sciences : CMLS · 2021Review
- Review
- Dopamine in Health and Disease: Much More Than a Neurotransmitter.Biomedicines · 2021Review
- Purinergic GPCR transmembrane residues involved in ligand recognition and dimerization.Methods in cell biology · 2021Review
Corrections and comments
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Authors and funding
16 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundG-protein-coupled receptors (GPCRs), in the form of monomers or homodimers that bind heterotrimeric G proteins, are fundamental in the transfer of extracellular stimuli to intracellular signaling pathways. Different GPCRs may also interact to form heteromers that are novel signaling units. Despite the exponential growth in the number of solved GPCR crystal structures, the structural properties of heteromers remain unknown.
resultsWe used single-particle tracking experiments in cells expressing functional adenosine A1-A2A receptors fused to fluorescent proteins to show the loss of Brownian movement of the A1 receptor in the presence of the A2A receptor, and a preponderance of cell surface 2:2 receptor heteromers (dimer of dimers). Using computer modeling, aided by bioluminescence resonance energy transfer assays to monitor receptor homomerization and heteromerization and G-protein coupling, we predict the interacting interfaces and propose a quaternary structure of the GPCR tetramer in complex with two G proteins.
conclusionsThe combination of results points to a molecular architecture formed by a rhombus-shaped heterotetramer, which is bound to two different interacting heterotrimeric G proteins (Gi and Gs). These novel results constitute an important advance in understanding the molecular intricacies involved in GPCR function.
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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.