Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/120611
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Navarro Brugal, Gemma | - |
dc.contributor.author | Cordomí, Arnau | - |
dc.contributor.author | Brugarolas Campillos, Marc | - |
dc.contributor.author | Moreno Guillén, Estefanía | - |
dc.contributor.author | Aguinaga Andrés, David | - |
dc.contributor.author | Pérez-Benito, Laura | - |
dc.contributor.author | Ferré, Sergi | - |
dc.contributor.author | Cortés Tejedor, Antonio | - |
dc.contributor.author | Casadó, Vicent | - |
dc.contributor.author | Mallol Montero, Josefa | - |
dc.contributor.author | Canela Campos, Enric I. | - |
dc.contributor.author | Lluís i Biset, Carme | - |
dc.contributor.author | Pardo, Leonardo | - |
dc.contributor.author | McCormick, Peter J. | - |
dc.contributor.author | Franco Fernández, Rafael | - |
dc.date.accessioned | 2018-03-12T12:29:24Z | - |
dc.date.available | 2018-03-12T12:29:24Z | - |
dc.date.issued | 2018-02-28 | - |
dc.identifier.issn | 1741-7007 | - |
dc.identifier.uri | http://hdl.handle.net/2445/120611 | - |
dc.description.abstract | BACKGROUND: G-protein-coupled receptor (GPCR) heteromeric complexes have distinct properties from homomeric GPCRs, giving rise to new receptor functionalities. Adenosine receptors (A1R or A2AR) can form A1R-A2AR heteromers (A1-A2AHet), and their activation leads to canonical G-protein-dependent (adenylate cyclase mediated) and -independent (β-arrestin mediated) signaling. Adenosine has different affinities for A1R and A2AR, allowing the heteromeric receptor to detect its concentration by integrating the downstream Gi- and Gs-dependent signals. cAMP accumulation and β-arrestin recruitment assays have shown that, within the complex, activation of A2AR impedes signaling via A1R. RESULTS: We examined the mechanism by which A1-A2AHet integrates Gi- and Gs-dependent signals. A1R blockade by A2AR in the A1-A2AHet is not observed in the absence of A2AR activation by agonists, in the absence of the C-terminal domain of A2AR, or in the presence of synthetic peptides that disrupt the heteromer interface of A1-A2AHet, indicating that signaling mediated by A1R and A2AR is controlled by both Gi and Gs proteins. CONCLUSIONS: We identified a new mechanism of signal transduction that implies a cross-communication between Gi and Gs proteins guided by the C-terminal tail of the A2AR. This mechanism provides the molecular basis for the operation of the A1-A2AHet as an adenosine concentration-sensing device that modulates the signals originating at both A1R and A2AR. | - |
dc.format.extent | 15 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | BioMed Central | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1186/s12915-018-0491-x | - |
dc.relation.ispartof | Bmc Biology, 2018, vol. 16, num. 1, p. 24 | - |
dc.relation.uri | https://doi.org/10.1186/s12915-018-0491-x | - |
dc.rights | cc-by (c) Navarro Brugal, Gemma et al., 2018 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es | - |
dc.source | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) | - |
dc.subject.classification | Adenosina | - |
dc.subject.classification | Receptors cel·lulars | - |
dc.subject.other | Adenosine | - |
dc.subject.other | Cell receptors | - |
dc.title | Cross-communication between Gi and Gs in a G-protein-coupled receptor heterotetramer guided by a receptor C-terminal domain | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 677608 | - |
dc.date.updated | 2018-03-12T12:29:24Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 29486745 | - |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
677608.pdf | 3.67 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License