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Identification of three residues essential for 5-hydroxytryptamine 2A-metabotropic glutamate 2 (5-HT2A·mGlu2) receptor heteromerization and Its psychoactive behavioral function

AutorPilar-Cuéllar, Fuencisla ; Callado, Luis F.; Milligan, Graeme; López-Giménez, Juan F. ; Meana, J. J.; González-Maeso, Javier
Fecha de publicación2012
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 287(53): 4430- 44319 (2012)
ResumenSerotonin and glutamate G protein-coupled receptor (GPCR) neurotransmission affects cognition and perception in humans and rodents. GPCRs are capable of forming heteromeric complexes that differentially alter cell signaling, but the role of this structural arrangement in modulating behavior remains unknown. Here, we identified three residues located at the intracellular end of transmembrane domain four that are necessary for the metabotropic glutamate 2 (mGlu2) receptor to be assembled as a GPCR heteromer with the serotonin 5-hydroxytryptamine 2A (5-HT2A) receptor in the mouse frontal cortex. Substitution of these residues (Ala-6774.40, Ala-6814.44, and Ala-6854.48) leads to absence of 5-HT2A·mGlu2 receptor complex formation, an effect that is associated with a decrease in their heteromeric ligand binding interaction. Disruption of heteromeric expression with mGlu2 attenuates the psychosis-like effects induced in mice by hallucinogenic 5-HT2A agonists. Furthermore, the ligand binding interaction between the components of the 5-HT2A·mGlu2 receptor heterocomplex is up-regulated in the frontal cortex of schizophrenic subjects as compared with controls. Together, these findings provide structural evidence for the unique behavioral function of a GPCR heteromer.
DescripciónEl pdf del artículo es la versión post-print.-- et al.
URIhttp://hdl.handle.net/10261/81506
DOI10.1074/jbc.M112.413161
Identificadoresdoi: 10.1074/jbc.M112.413161
issn: 0021-9258
e-issn: 1083-351X
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