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Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis


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dc.creator Martínez Fábregas, Jonathan es
dc.creator Díaz Moreno, Irene es
dc.creator González Arzola, Katiuska es
dc.creator Janocha, Simon es
dc.creator Navarro Carruesco, José Antonio es
dc.creator Hervás Morón, Manuel es
dc.creator Bernhardt, Rita es
dc.creator Velázquez Campoy, Adrián es
dc.creator Díaz Quintana, Antonio Jesús es
dc.creator Rosa Acosta, Miguel Ángel de la es 2017-11-28T15:46:38Z 2017-11-28T15:46:38Z 2014
dc.identifier.citation Martínez Fábregas, J., Díaz Moreno, I., González Arzola, K., Janocha, S., Navarro Carruesco, J.A., Hervás Morón, M.,...,Rosa Acosta, M.Á.d.l. (2014). Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis. Molecular and Cellular Proteomics, 13 (6), 1439-1456.
dc.identifier.issn 1535-9476 (impreso) es
dc.identifier.issn 1535-9484 (electrónico) es
dc.description.abstract Since the first description of apoptosis four decades ago, great efforts have been made to elucidate, both in vivo and in vitro, the molecular mechanisms involved in its regulation. Although the role of cytochrome c during apoptosis is well-established, relatively little is known about its participation in signaling pathways in vivo due to its essential role during respiration. To better understand the role of cytochrome c in the onset of apoptosis, a proteomic approach based on affinity chromatography with cytochrome c as bait was used in this study. In this approach, novel cytochrome c interaction partners were identified whose in vivo interaction, as well as cellular localization, were facilitated through bimolecular fluorescence complementation. Modeling of the complexes interface between cytochrome c and its counterparts indicated the involvement of the surface surrounding the heme crevice of cytochrome c, in agreement with the vast majority of known redox adducts of cytochrome c. However, in contrast to the high turnover rate of the mitochondrial cytochrome c redox adducts, those occurring under apoptosis lead to the formation of stable nucleo-cytoplasmic ensembles, as inferred mainly from surface plasmon resonance and nuclear magnetic resonance measurements, which have permitted us to corroborate the formation of such complexes in vitro. The results obtained suggest that human cytochrome c interacts with pro-survival, anti-apoptotic proteins following its release into the cytoplasm. Thus, cytochrome c may interfere with cell survival pathways and unlock apoptosis in order to prevent the spatial and temporal co-existence of antagonist signals. es
dc.description.sponsorship Ministerio de Ciencia e Innovación BFU2009-07190, BFU2012-31670 es
dc.description.sponsorship Junta de Andalucía BIO198 es
dc.format application/pdf es
dc.language.iso eng es
dc.publisher American Society for Biochemistry and Molecular Biology es
dc.relation.ispartof Molecular and Cellular Proteomics, 13 (6), 1439-1456.
dc.rights Attribution-NonCommercial-NoDerivatives 4.0 Internacional *
dc.rights.uri *
dc.subject 2-D Gel electrophoresis es
dc.subject Apoptosis es
dc.subject Cell death es
dc.subject Networks es
dc.subject Protein-protein interactions es
dc.title Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis es
dc.type info:eu-repo/semantics/article es
dc.type.version info:eu-repo/semantics/submittedVersion es
dc.rights.accessrights info:eu-repo/semantics/openAccess es
dc.contributor.affiliation Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular es
dc.relation.projectID BFU2009-07190 es
dc.relation.projectID BFU2012-31670 es
dc.relation.projectID BIO198 es
dc.relation.publisherversion es
dc.identifier.doi 10.1074/mcp.M113.034322 es
idus.format.extent 59 p. es
dc.journaltitle Molecular and Cellular Proteomics es
dc.publication.volumen 13 es
dc.publication.issue 6 es
dc.publication.initialPage 1439 es
dc.publication.endPage 1456 es
dc.contributor.funder Ministerio de Ciencia e Innovación (MICIN). España
dc.contributor.funder Junta de Andalucía
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