ArticleNature structural & molecular biology2022
Structural insight into apelin receptor-G protein stoichiometry.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- Article
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- Structural characterization of kappa-opioid receptor dimer in complex with two G proteins.Nature communications · 2026Article
- International Union of Basic and Clinical Pharmacology. CXXI. Apelin receptor pharmacology in the human cardiovascular system and emerging clinical applications.Pharmacological reviews · 2026Review
- Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.Nature communications · 2026Article
- Allosteric activation of the glutamate receptor mGlu2 by the serotonin receptor 5-HTNature communications · 2026Article
- Molecular basis of antagonism of the dimeric human arginine vasopressin receptor 1A.Nature communications · 2026Article
- GPCR Heterodimers: Implications for Biased Signaling.Handbook of experimental pharmacology · 2026Review
- Structural basis of protease-activated receptor 2 activation and biased agonism.Cell discovery · 2025Article
- Combining Cryo-EM with Computational Approaches To Revolutionize Structural Biology.The protein journal · 2025Review
- A biased allosteric modulator functions as a molecular glue to induce βResearch square · 2025Article
- Constitutive arrestin recruitment by orphan GPR52 via an atypical binding mode.Cell research · 2025Article
- State-Specific Peptide Design Targeting G Protein-Coupled Receptors.Journal of chemical information and modeling · 2025Article
- A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025Article
- Stabilized DNature communications · 2025Article
- Constitutively active orphan G protein-coupled receptors through the lenses of cryo-electron microscopy.The Journal of biological chemistry · 2025Review
- Mechanism and function of GPR3 regulated by a negative allosteric modulator.Nature communications · 2025Article
- Mechanistic insights into the versatile stoichiometry and biased signaling of the apelin receptor-arrestin complex.Nature communications · 2025Article
- Locomotor activity depends on β-arrestin recruitment by the dopamine DPharmacological research · 2025Article
- Multiscale biased chemical space remodeling for developing APLNR agonists with anti-HFpEF efficacy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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Authors and funding
19 authors at 4 institutions in 3 countries.
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Abstract
The technique of cryogenic-electron microscopy (cryo-EM) has revolutionized the field of membrane protein structure and function with a focus on the dominantly observed molecular species. This report describes the structural characterization of a fully active human apelin receptor (APJR) complexed with heterotrimeric G protein observed in both 2:1 and 1:1 stoichiometric ratios. We use cryo-EM single-particle analysis to determine the structural details of both species from the same sample preparation. Protein preparations, in the presence of the endogenous peptide ligand ELA or a synthetic small molecule, both demonstrate these mixed stoichiometric states. Structural differences in G protein engagement between dimeric and monomeric APJR suggest a role for the stoichiometry of G protein-coupled receptor- (GPCR-)G protein coupling on downstream signaling and receptor pharmacology. Furthermore, a small, hydrophobic dimer interface provides a starting framework for additional class A GPCR dimerization studies. Together, these findings uncover a mechanism of versatile regulation through oligomerization by which GPCRs can modulate their signaling.
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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.