ArticleThe Journal of biological chemistry2015
Single molecule analysis of functionally asymmetric G protein-coupled receptor (GPCR) oligomers reveals diverse spatial and structural assemblies.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Review
- Conformational equilibria in the activation of cystine-knot hormone receptors.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structure of an LGR dimer, an evolutionary predecessor of glycoprotein hormone receptors.Nature communications · 2025Article
- Stabilized DNature communications · 2025Article
- Single-molecule localization microscopy as a tool to quantify di/oligomerization of receptor tyrosine kinases and G protein-coupled receptors.Molecular pharmacology · 2025Review
- Advancements and Practical Considerations for Biophysical Research: Navigating the Challenges and Future of Super-resolution Microscopy.Chemical & biomedical imaging · 2024Review
- Article
- Granulosa Cells Alone, Without Theca Cells, Can Mediate LH-induced Oocyte Meiotic Resumption.Endocrinology · 2024Article
- Dynamic Dimerization of Chemokine Receptors and Potential Inhibitory Role of Their Truncated Isoforms Revealed through Combinatorial Prediction.International journal of molecular sciences · 2023Article
- Allosteric modulation of gonadotropin receptors.Frontiers in endocrinology · 2023Review
- Single-molecule counting applied to the study of GPCR oligomerization.Biophysical journal · 2022Review
- Functional rewiring of G protein-coupled receptor signaling in human labor.Cell reports · 2022Article
- Regulation of antral follicular growth by an interplay between gonadotropins and their receptors.Journal of assisted reproduction and genetics · 2022Review
- Human FSH Glycoform α-Subunit AsparagineFrontiers in endocrinology · 2022Article
- Integration and Spatial Organization of Signaling by G Protein-Coupled Receptor Homo- and Heterodimers.Biomolecules · 2021Review
- Article
- Receptor-Receptor Interactions and Glial Cell Functions with a Special Focus on G Protein-Coupled Receptors.International journal of molecular sciences · 2021Review
- The Luteinizing Hormone Receptor Knockout Mouse as a Tool to Probe the In Vivo Actions of Gonadotropic Hormones/Receptors in Females.Endocrinology · 2021Article
- Differential FSH Glycosylation Modulates FSHR Oligomerization and Subsequent cAMP Signaling.Frontiers in endocrinology · 2021Article
- Identification of Key Receptor Residues Discriminating Human Chorionic Gonadotropin (hCG)- and Luteinizing Hormone (LH)-Specific Signaling.International journal of molecular sciences · 2020Article
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4 authors.
Funding
Abstract
Formation of G protein-coupled receptors (GPCRs) into dimers and higher order oligomers represents a key mechanism in pleiotropic signaling, yet how individual protomers function within oligomers remains poorly understood. We present a super-resolution imaging approach, resolving single GPCR molecules to ∼ 8 nm resolution in functional asymmetric dimers and oligomers using dual-color photoactivatable dyes and localization microscopy (PD-PALM). PD-PALM of two functionally defined mutant luteinizing hormone receptors (LHRs), a ligand-binding deficient receptor (LHR(B-)) and a signaling-deficient (LHR(S-)) receptor, which only function via intermolecular cooperation, favored oligomeric over dimeric formation. PD-PALM imaging of trimers and tetramers revealed specific spatial organizations of individual protomers in complexes where the ratiometric composition of LHR(B-) to LHR(S-) modulated ligand-induced signal sensitivity. Structural modeling of asymmetric LHR oligomers strongly aligned with PD-PALM-imaged spatial arrangements, identifying multiple possible helix interfaces mediating inter-protomer associations. Our findings reveal that diverse spatial and structural assemblies mediating GPCR oligomerization may acutely fine-tune the cellular signaling profile.
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