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dc.contributor.authorDenuc, Amanda
dc.contributor.authorNunez, Estefania 
dc.contributor.authorCalvo, Enrique 
dc.contributor.authorLoureiro, Marta 
dc.contributor.authorMiro-Casas, Elisabet
dc.contributor.authorGuaras, Adela 
dc.contributor.authorVazquez, Jesus 
dc.contributor.authorGarcia-Dorado, David
dc.date.accessioned2017-10-30T13:32:25Z
dc.date.available2017-10-30T13:32:25Z
dc.date.issued2016
dc.identifierISI:000374835800003
dc.identifier.citationJ Cell Mol Med. 2016; 20(5):794-803
dc.identifier.issn1582-4934
dc.identifier.urihttp://hdl.handle.net/20.500.12105/5235
dc.description.abstractConnexin 43 (Cx43), the gap junction protein involved in cell-to-cell coupling in the heart, is also present in the subsarcolemmal fraction of cardiomyocyte mitochondria. It has been described to regulate mitochondrial potassium influx and respiration and to be important for ischaemic preconditioning protection, although the molecular effectors involved are not fully characterized. In this study, we looked for potential partners of mitochondrial Cx43 in an attempt to identify new molecular pathways for cardioprotection. Mass spectrometry analysis of native immunoprecipitated mitochondrial extracts showed that Cx43 interacts with several proteins related with mitochondrial function and metabolism. Among them, we selected for further analysis only those present in the subsarcolemmal mitochondrial fraction and known to be related with the respiratory chain. Apoptosis-inducing factor (AIF) and the beta-subunit of the electron-transfer protein (ETFB), two proteins unrelated to date with Cx43, fulfilled these conditions, and their interaction with Cx43 was proven by direct and reverse co-immunoprecipitation. Furthermore, a previously unknown molecular interaction between AIF and ETFB was established, and protein content and sub-cellular localization appeared to be independent from the presence of Cx43. Our results identify new protein-protein interactions between AIF-Cx43, ETFB-Cx43 and AIF-ETFB as possible players in the regulation of the mitochondrial redox state.
dc.description.sponsorshipWe thank Angeles Rojas for technical assistance and Marisol Ruiz-Meana for critical discussion of the article. AD, EN, EC and ML performed the research; AD, EN, EC, ML, JV and DGD analysed the data; AD, JV and DGD wrote the article. All authors approved the final version. This work was funded by CD12/00493 Sara Borrell grant from the Institute of Health Carlos III to A. D and RIC RD12/0042/0021 and SAF 2008-03067 from the Spanish Ministry of Science.
dc.language.isoeng
dc.publisherWILEY
dc.relation.isversionofPublisher's version
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectconnexin 43
dc.subjectapoptosis-inducing factor
dc.subjectelectron-transfer protein
dc.subjectmitochondria
dc.subjectcardiomyocyte
dc.subjectAPOPTOSIS-INDUCING FACTOR
dc.subjectELECTRON-TRANSFER FLAVOPROTEIN
dc.subjectCARDIOMYOCYTE MITOCHONDRIA
dc.subjectGAP-JUNCTIONS
dc.subjectMICE
dc.subjectOXYGEN
dc.subjectCX43
dc.subjectPHOSPHORYLATION
dc.subjectCONTRIBUTES
dc.subjectMICROSCOPY
dc.titleNew protein-protein interactions of mitochondrial connexin 43 in mouse heart
dc.typeArtículo
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID26915330
dc.format.volume20
dc.format.page794-803
dc.identifier.doi10.1111/jcmm.12792
dc.contributor.funderInstituto de Salud Carlos III - ISCIII
dc.contributor.funderMinisterio de Ciencia e Innovación (España)
dc.description.peerreviewed
dc.relation.publisherversionhttps://doi.org/10.1111/jcmm.12792
dc.identifier.journalJournal of Cellular and Molecular Medicine
dc.repisalud.orgCNICCNIC::Grupos de investigación::Proteómica cardiovascular
dc.repisalud.orgCNICCNIC::Unidades técnicas::Proteómica / Metabolómica
dc.repisalud.institucionCNIC
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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