Mostra el registre d'ítem simple

dc.contributor.authorTena Campos, Mercè
dc.contributor.authorRamon Portés, Eva
dc.contributor.authorBorroto Escuela, Dasiel Óscar
dc.contributor.authorFuxe, Kjell
dc.contributor.authorGarriga Solé, Pere
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2016-01-08T08:22:59Z
dc.date.available2017-12-01T01:30:25Z
dc.date.issued2015-12-01
dc.identifier.citationTena, M., Ramon, E., Borroto, D., Fuxe, K., Garriga, P. The zinc binding receptor GPR39 interacts with 5-HT1A and GalR(1) to form dynamic heteroreceptor complexes with signaling diversity. "Biochimica et biophysica acta. Molecular basis of disease", 01 Desembre 2015, vol. 1852, núm. 12, p. 2585-2592.
dc.identifier.issn0925-4439
dc.identifier.urihttp://hdl.handle.net/2117/81129
dc.description.abstractGPR39 is a class A G protein-coupled receptor involved in zinc binding and glucose homeostasis regulation, among other physiological processes. GPR39 was originally thought to be the receptor for obestatin peptide but this view has been challenged. However, activation of this receptor by zinc has been clearly established. Recent studies suggest that low GPR39 expression, due to deficient zinc levels, is involved in major depressive disorder. We have previously reported that zinc can alter receptor-receptor interactions and favor specific receptor interactions. In order to unravel the effect of zinc on specific G protein-coupled receptor association processes, we have performed FRET and co-immunopurification studies with GPR39 and 5-HT1A and GalR(1) which have been shown to dimerize. Our results suggest that zinc can modulate the formation of specific 5-HT1A-GPR39 and GalR(1)-5-HT1A-GPR39 heteroreceptor complexes under our experimental conditions.; We have analyzed the differences in signaling between the mono-homomeric receptors 5-HT1A, GalR(1) and GPR39 and the heteroreceptor complexes between them Our results show that the GPR39-5-HT1A heterocomplex has additive functionalities when compared to the monomeric-homomeric receptors upon receptor activation. In addition, the heterocomplex including also GalR(1) shows a different behavior, upon exposure to the same agonists. Furthermore, these processes appear to be regulated by zinc. These findings provide a rationale for the antidepressive effect widely described for zinc because pro-depressive heterocomplexes are predominant at low zinc concentration levels. (C) 2015 Elsevier B.V. All rights reserved.
dc.format.extent8 p.
dc.language.isoeng
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria química
dc.subject.lcshG proteins--Receptors
dc.subject.otherDepression
dc.subject.otherG protein-coupled receptor
dc.subject.otherHeterooligomerization
dc.subject.otherPurified receptor
dc.subject.otherSignal transduction
dc.subject.otherZinc
dc.subject.otherG-Protein
dc.subject.otherdepression
dc.subject.otherobestatin
dc.subject.othermouse
dc.titleThe zinc binding receptor GPR39 interacts with 5-HT1A and GalR(1) to form dynamic heteroreceptor complexes with signaling diversity
dc.typeArticle
dc.subject.lemacProteïnes G -- Receptors
dc.contributor.groupUniversitat Politècnica de Catalunya. GBMI - Grup de Biotecnologia Molecular i Industrial
dc.identifier.doi10.1016/j.bbadis.2015.09.003
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S0925443915002677
dc.rights.accessOpen Access
local.identifier.drac17269808
dc.description.versionPostprint (author's final draft)
local.citation.authorTena, M.; Ramon, E.; Borroto, D.; Fuxe, K.; Garriga, P.
local.citation.publicationNameBiochimica et biophysica acta. Molecular basis of disease
local.citation.volume1852
local.citation.number12
local.citation.startingPage2585
local.citation.endingPage2592


Fitxers d'aquest items

Thumbnail

Aquest ítem apareix a les col·leccions següents

Mostra el registre d'ítem simple