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http://hdl.handle.net/2445/189394
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DC Field | Value | Language |
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dc.contributor.author | De Oliveira, Paulo A. | - |
dc.contributor.author | Moreno Guillén, Estefanía | - |
dc.contributor.author | Casajuana-Martin, Nil | - |
dc.contributor.author | Casadó Anguera, Verònica | - |
dc.contributor.author | Cai, Ning-Sheng | - |
dc.contributor.author | Camacho-Hernandez, Gisela Andrea | - |
dc.contributor.author | Zhu, Hu | - |
dc.contributor.author | Bonifazi, Alessandro | - |
dc.contributor.author | Hall, Matthew D. | - |
dc.contributor.author | Weinshenker, David | - |
dc.contributor.author | Newman, Amy Hauck | - |
dc.contributor.author | Logothetis, Diomedes E. | - |
dc.contributor.author | Casadó, Vicent | - |
dc.contributor.author | Plant, Leigh D. | - |
dc.contributor.author | Pardo, Leonardo | - |
dc.contributor.author | Ferré, Sergi | - |
dc.date.accessioned | 2022-09-28T14:42:34Z | - |
dc.date.available | 2022-09-28T14:42:34Z | - |
dc.date.issued | 2022-06-22 | - |
dc.identifier.issn | 1043-6618 | - |
dc.identifier.uri | http://hdl.handle.net/2445/189394 | - |
dc.description.abstract | Recent studies have proposed that heteromers of μ-opioid receptors (MORs) and galanin Gal1 receptors (Gal1Rs) localized in the mesencephalon mediate the dopaminergic effects of opioids. The present study reports converging evidence, using a peptide-interfering approach combined with biophysical and biochemical techniques, including total internal reflection fluorescence microscopy, for a predominant homodimeric structure of MOR and Gal1R when expressed individually, and for their preference to form functional heterotetramers when co-expressed. Results show that a heteromerization-dependent change in the Gal1R homodimeric interface leads to a switch in G-protein coupling from inhibitory Gi to stimulatory Gs proteins. The MOR-Gal1R heterotetramer, which is thus bound to Gs via the Gal1R homodimer and Gi via the MOR homodimer, provides the framework for a canonical Gs-Gi antagonist interaction at the adenylyl cyclase level. These novel results shed light on the intense debate about the oligomeric quaternary structure of G protein-coupled receptors, their predilection for heteromer formation, and the resulting functional significance. | - |
dc.format.extent | 14 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Elsevier B.V. | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1016/j.phrs.2022.106322 | - |
dc.relation.ispartof | Pharmacological Research, 2022, vol. 182, p. 106322 | - |
dc.relation.uri | https://doi.org/10.1016/j.phrs.2022.106322 | - |
dc.rights | cc-by-nc-nd (c) De Oliveira, Paulo A. et al., 2022 | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/4.0/ | - |
dc.source | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) | - |
dc.subject.classification | Oligòmers | - |
dc.subject.classification | Proteïnes G | - |
dc.subject.other | Oligomers | - |
dc.subject.other | G Proteins | - |
dc.title | Preferential Gs protein coupling of the galanin Gal1 receptor in the μ-opioid-Gal1 receptor heterotetramer | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 723994 | - |
dc.date.updated | 2022-09-28T14:42:34Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) |
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723994.pdf | 6.94 MB | Adobe PDF | View/Open |
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