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| Título: | Evidence for distinct antagonist-revealed functional states of 5-hydroxytryptamine(2A) receptor homodimers |
Autor: | Vilaró, Maria Teresa CSIC ORCID; Mengod Los Arcos, Guadalupe CSIC ORCID; Loza, María Isabel | Fecha de publicación: | 11-mar-2009 | Editor: | American Society for Pharmacology and Experimental Therapeutics | Citación: | Molecular Pharmacology 75(6): 1380-1391 (2009) | Resumen: | The serotonin (5-hydroxytryptamine; 5-HT) 2A receptor is a cell surface class A G protein-coupled receptor that regulates a multitude of physiological functions of the body and is a target for antipsychotic drugs. Here we found by means of fluorescence resonance energy transfer and immunoprecipitation studies that the 5-HT2A -receptor homodimerized in live cells, which we linked with its antagonist-dependent fingerprint in both binding and receptor signaling. Some antagonists, like the atypical antipsychotics clozapine and risperidone, differentiate themselves from others, like the typical antipsychotic haloperidol, antagonizing these 5-HT2A receptor-mediated functions in a pathway-specific manner, explained here by a new model of multiple active interconvertible conformations at dimeric receptors. | Descripción: | et al. | Versión del editor: | http://dx.doi.org/10.1124/mol.108.054395 | URI: | http://hdl.handle.net/10261/31994 | DOI: | 10.1124/mol.108.054395 | ISSN: | 0026-895X | E-ISSN: | 1521-0111 |
| Aparece en las colecciones: | (IIBB) Artículos |
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| accesoRestringido.pdf | 15,38 kB | Adobe PDF |  Visualizar/Abrir |
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