ArticleThe Journal of biological chemistry2012
Functional homomers and heteromers of dopamine D2L and D3 receptors co-exist at the cell surface.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Mechanistic and therapeutic insights into class A GPCR dimers in neuropsychiatric disorders.npj drug discovery · 2026Review
- The Heteromeric Dopamine Receptor D2:D3 Controls the Gut Recruitment and Suppressive Activity of Regulatory T-Cells.International journal of molecular sciences · 2025Article
- Pharmacological targeting of G protein-coupled receptor heteromers.Pharmacological research · 2022Article
- Chirality of Novel Bitopic Agonists Determines Unique Pharmacology at the Dopamine D3 Receptor.Biomolecules · 2021Article
- Lanthanide-Based Optical Probes of Biological Systems.Cell chemical biology · 2020Review
- Reinterpreting anomalous competitive binding experiments within G protein-coupled receptor homodimers using a dimer receptor model.Pharmacological research · 2019Article
- The Endocannabinoid System as a Target in Cancer Diseases: Are We There Yet?Frontiers in pharmacology · 2019Review
- The First Negative Allosteric Modulator for Dopamine DMolecular pharmacology · 2017Review
- A Molecular Basis for Selective Antagonist Destabilization of Dopamine DScientific reports · 2017Article
- Methods used to study the oligomeric structure of G-protein-coupled receptors.Bioscience reports · 2017Review
- Visualization and ligand-induced modulation of dopamine receptor dimerization at the single molecule level.Scientific reports · 2016Article
- Membrane omega-3 fatty acids modulate the oligomerisation kinetics of adenosine A2A and dopamine D2 receptors.Scientific reports · 2016Article
- Analysis of Human Dopamine D3 Receptor Quaternary Structure.The Journal of biological chemistry · 2015Article
- Distinct Agonist Regulation of Muscarinic Acetylcholine M2-M3 Heteromers and Their Corresponding Homomers.The Journal of biological chemistry · 2015Article
- A Broad G Protein-Coupled Receptor Internalization Assay that Combines SNAP-Tag Labeling, Diffusion-Enhanced Resonance Energy Transfer, and a Highly Emissive Terbium Cryptate.Frontiers in endocrinology · 2015Article
- The G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components.International journal of molecular sciences · 2014Article
- Heteromeric dopamine receptor signaling complexes: emerging neurobiology and disease relevance.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Review
- Biophysical Detection of Diversity and Bias in GPCR Function.Frontiers in endocrinology · 2014Review
- Glioblastoma treatment using perphenazine to block the subventricular zone's tumor trophic functions.Journal of neuro-oncology · 2014Review
- Reduction of cocaine self-administration and D3 receptor-mediated behavior by two novel dopamine D3 receptor-selective partial agonists, OS-3-106 and WW-III-55.The Journal of pharmacology and experimental therapeutics · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Human dopamine D(2long) and D(3) receptors were modified by N-terminal addition of SNAP or CLIP forms of O(6)-alkylguanine-DNA-alkyltransferase plus a peptide epitope tag. Cells able to express each of these four constructs only upon addition of an antibiotic were established and used to confirm regulated and inducible control of expression, the specificity of SNAP and CLIP tag covalent labeling reagents, and based on homogenous time-resolved fluorescence resonance energy transfer, the presence of cell surface D(2long) and D(3) receptor homomers. Following constitutive expression of reciprocal constructs, potentially capable of forming and reporting the presence of cell surface D(2long)-D(3) heteromers, individual clones were assessed for levels of expression of the constitutively expressed protomer. This was unaffected by induction of the partner protomer and the level of expression of the partner required to generate detectable cell surface D(2long)-D(3) heteromers was defined. Such homomers and heteromers were found to co-exist and using a reconstitution of function approach both homomers and heteromers of D(2long) and D(3) receptors were shown to be functional, potentially via trans-activation of associated G protein. These studies demonstrate the ability of dopamine D(2long) and D(3) receptors to form both homomers and heteromers, and show that in cells expressing each subtype a complex mixture of homomers and heteromers co-exists at steady state. These data are of potential importance both to disorders in which D(2long) and D(3) receptors are implicated, like schizophrenia and Parkinson disease, and also to drugs exerting their actions via these sites.
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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.