ArticleNature communications2025
Single-molecule characterization of opioid receptor heterodimers reveals soluble µ-δ dimer blocker peptide alleviates morphine tolerance.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- Emerging Insights into the Distinct Pharmacological Mechanisms of Buprenorphine.Journal of chemical information and modeling · 2026Article
- Structural characterization of kappa-opioid receptor dimer in complex with two G proteins.Nature communications · 2026Article
- Development of ultrafast single fluorescent-molecule imaging and its application to unravel plasma membrane structure and function in live cells.Biophysics and physicobiology · 2026Article
- Coactivation of CB1 and GPR55 promotes GABA release and motor behavior at striatonigral terminals through increased dimerization induced by CB1 activation.Frontiers in molecular neuroscience · 2026Article
- Single-molecule methods for characterizing receptor dimers reveal metastable opioid receptor homodimers that induce functional modulation.Nature communications · 2025Article
- Functional significance of opioid receptor homomers and heteromers.Nature communications · 2025Article
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Authors and funding
11 authors.
Funding
Abstract
Heterodimerization of opioid receptors (ORs), MOR, KOR, and DOR, is implied in their functional regulation and diversification, and thus its understanding is crucial for developing better analgesic treatments. However, our knowledge on OR heterodimerization/heterodimers remains limited. Here, using single-molecule imaging and functional analysis, we find that MOR, the main morphine receptor, repeatedly forms transient (≈250 ms) heterodimers with DOR every 1-10 seconds, but not with KOR, whereas DOR and KOR also form transient heterodimers. We obtain all the heterodimer-monomer equilibrium constants and rate constants with/without agonists. We identify the critical heterodimer binding sites in the extracellular domains, in addition to the less-specific transmembrane domains, and develop soluble peptide blockers for MOR-DOR and DOR-KOR heterodimerization, using amino-acid sequences mimicking the extracellular binding sites. With these peptide blockers, we dissect the monomer/dimer roles in OR internalization and signaling. The soluble MOR-DOR heterodimer blocker reduces the development of long-term morphine tolerance in mice.
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