Dual coupling of the cloned 5-HT1A receptor to both adenylyl cyclase and phospholipase C is mediated via the same Gi protein.

Détails

ID Serval
serval:BIB_4EE567F64890
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Dual coupling of the cloned 5-HT1A receptor to both adenylyl cyclase and phospholipase C is mediated via the same Gi protein.
Périodique
Cellular Signalling
Auteur(s)
Fargin A., Yamamoto K., Cotecchia S., Goldsmith P.K., Spiegel A.M., Lapetina E.G., Caron M.G., Lefkowitz R.J.
ISSN
0898-6568 (Print)
ISSN-L
0898-6568
Statut éditorial
Publié
Date de publication
1991
Volume
3
Numéro
6
Pages
547-557
Langue
anglais
Résumé
The cloned 5-HT1A receptor, stably expressed in HeLa cells, has been shown to mediate the effects of 5-hydroxytryptamine (5-HT) to inhibit cAMP formation and to stimulate the hydrolysis of phosphatidylinositol. Both responses were found to be pertussis toxin sensitive. We have examined these two responses in membranes derived from these cells and show that the 5-HT1A receptor can directly regulate the activity of adenylyl cyclase and phospholipase C in response to agonist. In order to examine whether the same or distinct guanine nucleotide-binding regulatory protein(s) (G protein) are involved in these two signal transduction pathways, we used anti-peptide antibodies recognizing the alpha-subunits of Gi1, Gi2, Gi3 as specific tools, since these pertussis toxin substrates are expressed in HeLa cells. These antibodies have previously been shown to prevent receptor-G protein coupling by binding to the regions of G proteins which are putatively involved in interaction with receptors. Our results indicate that the Gi proteins, but preferentially Gi3, mediate the effects of 5-HT both to inhibit adenylyl cyclase and to stimulate phospholipase C. These findings demonstrate that the same receptor interacting with the same G protein can regulate several distinct effector molecules.
Mots-clé
Adenylate Cyclase/antagonists & inhibitors, Adenylate Cyclase/metabolism, Adenylate Cyclase Toxin, Animals, Cricetinae, GTP-Binding Proteins/metabolism, HeLa Cells, Humans, Pertussis Toxin, Receptors, Serotonin/metabolism, Signal Transduction, Type C Phospholipases/metabolism, Virulence Factors, Bordetella/pharmacology
Pubmed
Web of science
Création de la notice
24/01/2008 11:05
Dernière modification de la notice
20/08/2019 14:04
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