Publication: Single-molecule analysis reveals agonist-specific dimer formation of µ-opioid receptors
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Issued Date
2020-09-01
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ISSN
15524469
15524450
15524450
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2-s2.0-85089620365
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Mahidol University
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SCOPUS
Bibliographic Citation
Nature Chemical Biology. Vol.16, No.9 (2020), 946-954
Suggested Citation
Jan Möller, Ali Isbilir, Titiwat Sungkaworn, Brendan Osberg, Christos Karathanasis, Vikram Sunkara, Eugene O. Grushevskyi, Andreas Bock, Paolo Annibale, Mike Heilemann, Christof Schütte, Martin J. Lohse Single-molecule analysis reveals agonist-specific dimer formation of µ-opioid receptors. Nature Chemical Biology. Vol.16, No.9 (2020), 946-954. doi:10.1038/s41589-020-0566-1 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/58965
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Title
Single-molecule analysis reveals agonist-specific dimer formation of µ-opioid receptors
Abstract
© 2020, The Author(s), under exclusive licence to Springer Nature America, Inc. G-protein-coupled receptors (GPCRs) are key signaling proteins that mostly function as monomers, but for several receptors constitutive dimer formation has been described and in some cases is essential for function. Using single-molecule microscopy combined with super-resolution techniques on intact cells, we describe here a dynamic monomer–dimer equilibrium of µ-opioid receptors (µORs), where dimer formation is driven by specific agonists. The agonist DAMGO, but not morphine, induces dimer formation in a process that correlates both temporally and in its agonist- and phosphorylation-dependence with β-arrestin2 binding to the receptors. This dimerization is independent from, but may precede, µOR internalization. These data suggest a new level of GPCR regulation that links dimer formation to specific agonists and their downstream signals. [Figure not available: see fulltext.].