ArticleNature communications2025
Structural insights into the regulation of monomeric and dimeric apelin receptor.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Agonist Binding Reshapes the Kinetic Landscape and Allosteric Communication of APLNR Toward Activation-Competent States.International journal of molecular sciences · 2026Article
- Protein Self-Interaction in Cellular Function and Network Evolution: Molecular Mechanisms, AI-Driven Insights, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- Mechanistic and therapeutic insights into class A GPCR dimers in neuropsychiatric disorders.npj drug discovery · 2026Review
- Structural characterization of kappa-opioid receptor dimer in complex with two G proteins.Nature communications · 2026Article
- Dynamic monomer-dimer transition in ligand-induced apelin receptor activation.Nature communications · 2026Article
- Nanobodies unlock new mechanisms to target G protein-coupled receptors.Molecular pharmacology · 2026Review
- The Role of the Apelin Receptor in the Pathophysiology of Pulmonary Arterial Hypertension.Cells · 2026Review
- Molecular basis of antagonism of the dimeric human arginine vasopressin receptor 1A.Nature communications · 2026Article
- A biased allosteric modulator functions as a molecular glue to induce βResearch square · 2025Article
- A biased allosteric modulator functions as a molecular glue to induce βbioRxiv : the preprint server for biology · 2025Article
- Mechanistic insights into the versatile stoichiometry and biased signaling of the apelin receptor-arrestin complex.Nature communications · 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
- New Insights Into Adipokines and the Tumor Microenvironment in Breast Cancer.Cancer control : journal of the Moffitt Cancer CenterReview
Corrections and comments
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Authors and funding
19 authors.
Funding
Abstract
The apelin receptor (APJR) emerges as a promising drug target for cardiovascular health and muscle regeneration. While prior research unveiled the structural versatility of APJR in coupling to Gi proteins as a monomer or dimer, the dynamic regulation within the APJR dimer during activation remains poorly understood. In this study, we present the structures of the APJR dimer and monomer complexed with its endogenous ligand apelin-13. In the dimeric structure, apelin-13 binds exclusively to one protomer that is coupled with Gi proteins, revealing a distinct ligand-binding behavior within APJR homodimers. Furthermore, binding of an antagonistic antibody induces a more compact dimerization by engaging both protomers. Notably, structural analyses of the APJR dimer complexed with an agonistic antibody, with or without Gi proteins, suggest that G protein coupling may promote the dissociation of the APJR dimer during activation. These findings underscore the intricate interplay between ligands, dimerization, and G protein coupling in regulating APJR signaling pathways.
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