ArticleScientific reports2016
Visualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 96 citations in OpenAlex.
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- Single-molecule localization microscopy as a tool to quantify di/oligomerization of receptor tyrosine kinases and G protein-coupled receptors.Molecular pharmacology · 2025Review
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- The chemokine receptor CCR5: multi-faceted hook for HIV-1.Retrovirology · 2024Review
- Non-canonical interplay between glutamatergic NMDA and dopamine receptors shapes synaptogenesis.Nature communications · 2024Article
- Fluorescence based HTS-compatible ligand binding assays for dopamine DFrontiers in molecular biosciences · 2023Article
- Biased signaling due to oligomerization of the G protein-coupled platelet-activating factor receptor.Nature communications · 2022Article
- Total Internal Reflection Fluorescence (TIRF) Microscopy.Current protocols · 2022Review
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- Exploring the signaling space of a GPCR using bivalent ligands with a rigid oligoproline backbone.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Modulation of adenosine A2a receptor oligomerization by receptor activation and PIPStructure (London, England : 1993) · 2021Article
- Bivalent ligands promote endosomal trafficking of the dopamine D3 receptor-neurotensin receptor 1 heterodimer.Communications biology · 2021Article
- Membrane Nanoscopic Organization of D2L Dopamine Receptor Probed by Quantum Dot Tracking.Membranes · 2021Article
- Homo-oligomerization of the human adenosine AeLife · 2021Article
- Single-molecule FRET imaging of GPCR dimers in living cells.Nature methods · 2021Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 2 countries.
Funding
Abstract
G protein-coupled receptors (GPCRs), including dopamine receptors, represent a group of important pharmacological targets. An increased formation of dopamine receptor D2 homodimers has been suggested to be associated with the pathophysiology of schizophrenia. Selective labeling and ligand-induced modulation of dimerization may therefore allow the investigation of the pathophysiological role of these dimers. Using TIRF microscopy at the single molecule level, transient formation of homodimers of dopamine receptors in the membrane of stably transfected CHO cells has been observed. The equilibrium between dimers and monomers was modulated by the binding of ligands; whereas antagonists showed a ratio that was identical to that of unliganded receptors, agonist-bound D2 receptor-ligand complexes resulted in an increase in dimerization. Addition of bivalent D2 receptor ligands also resulted in a large increase in D2 receptor dimers. A physical interaction between the protomers was confirmed using high resolution cryogenic localization microscopy, with ca. 9 nm between the centers of mass.
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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.