The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Time-resolved FRET between GPCR ligands reveals oligomers in native tissues
Open accessAbstract
G protein–coupled receptor (GPCR) oligomers have been proposed to play critical roles in cell signaling, but confirmation of their existence in a native context remains elusive, as no direct interactions between receptors have been reported. To demonstrate their presence in native tissues, we developed a time-resolved FRET strategy that is based on receptor labeling with selective fluorescent ligands. Specific FRET signals were observed with four different receptors expressed in cell lines, consistent with their dimeric or oligomeric nature in these transfected cells. More notably, the comparison between FRET signals measured with sets of fluorescent agonists and antagonists was consistent with an asymmetric relationship of the two protomers in an activated GPCR dimer. Finally, we applied the strategy to native tissues and succeeded in demonstrating the presence of oxytocin receptor dimers and/or oligomers in mammary gland.
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Cites
G Protein-Coupled Receptor Allosterism and Complexing
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Self-citationBuilding a new conceptual framework for receptor heteromers
Ferré, S., Baler, R., Bouvier, M., Caron, M. G., Devi, L. A., Durroux, T., Fuxe, K., George, S. R., Javitch, J. A., Lohse, M. J., et al. (2009) · Nature Chemical Biology · doi:10.1038/nchembio0309-131 · Cited by 394
Self-citationA role for heterodimerization of μ and δ opiate receptors in enhancing morphine analgesia
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A heterodimer-selective agonist shows in vivo relevance of G protein-coupled receptor dimers
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Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation
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Dopamine D2 receptors form higher order oligomers at physiological expression levels
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Beaulieu, J., Espinoza, S., & Gainetdinov, R. R. (2015) · British Journal of Pharmacology · doi:10.1111/bph.12906 · Cited by 521
Oxytocin and Vasopressin Agonists and Antagonists as Research Tools and Potential Therapeutics
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Self-citationG protein-coupled receptor heteromers
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Metadata
- Authors
- Albizu, L., Cottet, M., Kralikova, M., Stoev, S., Seyer, R., Brabet, I., Roux, T., Bazin, H., Bourrier, E., Lamarque, L., Breton, C., Rives, M.-L., Newman, A., Javitch, J., Trinquet, E., Manning, M., Pin, J.-P., Mouillac, B., & Durroux, T.
- Venue
- Nature Chemical Biology
- Published
- 2010-07-11
- Volume
- 6
- Issue
- 8
- Pages
- 587-594
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1971256251
- Cited by
- 340
- References
- 50
- FWCI
- 14.89
- Type
- journal article
- Language
- en
- Open access
- green
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- Albizu, L., Cottet, M., Kralikova, M., Stoev, S., Seyer, R., Brabet, I., Roux, T., Bazin, H., Bourrier, E., Lamarque, L., Breton, C., Rives, M.-L., Newman, A., Javitch, J., Trinquet, E., Manning, M., Pin, J.-P., Mouillac, B., & Durroux, T. (2010). Time-resolved FRET between GPCR ligands reveals oligomers in native tissues. Nature Chemical Biology. https://doi.org/10.1038/nchembio.396
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