Evidence for distinct antagonist-revealed functional states of 5-hydroxytryptamine2A receptor homodimers

José Brea, Marián Castro, Jesús Giraldo, Juan F. López-Giménez, Juan Fernando Padín, Fátima Quintián, Maria Isabel Cadavid, Maria Teresa Vilaró, Guadalupe Mengod, Kelly A. Berg, William P. Clarke, Jean Pierre Vilardaga, Graeme Milligan, Maria Isabel Loza

Producción científica: Articlerevisión exhaustiva

57 Citas (Scopus)


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.

Idioma originalEnglish (US)
Páginas (desde-hasta)1380-1391
Número de páginas12
PublicaciónMolecular pharmacology
EstadoPublished - jun 2009

ASJC Scopus subject areas

  • Molecular Medicine
  • Pharmacology


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