Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.12530/42048
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dc.contributor.authorPérez-Pérez, Rafael
dc.contributor.authorLobo-Jarne, Teresa
dc.contributor.authorMilenkovic, Dusanka
dc.contributor.authorMourier, Arnaud
dc.contributor.authorBratic, Ana
dc.contributor.authorGarcía-Bartolomé, Alberto
dc.contributor.authorFernández-Vizarra, Erika
dc.contributor.authorCadenas, Susana
dc.contributor.authorDelmiro, Aitor
dc.contributor.authorGarcía-Consuegra, Inés
dc.contributor.authorArenas, Joaquín
dc.contributor.authorMartín, Miguel A
dc.contributor.authorLarsson, Nils-Göran
dc.contributor.authorUgalde, Cristina
dc.date.accessioned2019-08-29T08:52:49Z-
dc.date.available2019-08-29T08:52:49Z-
dc.date.issued2016
dc.identifier.citationCell Rep.2016 08;(16)9:2387-98
dc.identifier.urihttps://hdl.handle.net/20.500.12530/42048-
dc.description.abstractMitochondrial respiratory chain (MRC) complexes I, III, and IV associate into a variety of supramolecular structures known as supercomplexes and respirasomes. While COX7A2L was originally described as a supercomplex-specific factor responsible for the dynamic association of complex IV into these structures to adapt MRC function to metabolic variations, this role has been disputed. Here, we further examine the functional significance of COX7A2L in the structural organization of the mammalian respiratory chain. As in the mouse, human COX7A2L binds primarily to free mitochondrial complex III and, to a minor extent, to complex IV to specifically promote the stabilization of the III2+IV supercomplex without affecting respirasome formation. Furthermore, COX7A2L does not affect the biogenesis, stabilization, and function of the individual oxidative phosphorylation complexes. These data show that independent regulatory mechanisms for the biogenesis and turnover of different MRC supercomplex structures co-exist.
dc.language.isoeng
dc.rightsopenAccess-
dc.subject.meshAnimals
dc.subject.meshElectron Transport
dc.subject.meshElectron Transport Complex I
dc.subject.meshElectron Transport Complex III
dc.subject.meshElectron Transport Complex IV
dc.subject.meshGene Expression
dc.subject.meshHEK293 Cells
dc.subject.meshHeLa Cells
dc.subject.meshHumans
dc.subject.meshMice
dc.subject.meshMitochondria, Heart
dc.subject.meshMitochondrial Membranes
dc.subject.meshMyocardium
dc.subject.meshProtein Binding
dc.subject.meshProtein Stability
dc.subject.meshOxidative Phosphorylation
dc.titleCOX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation.
dc.typeArtículo
dc.identifier.pubmedID27545886
dc.format.volume16
dc.format.page2387-98
dc.identifier.e-issn2211-1247
dc.identifier.journalCell reports
dc.identifier.doi10.1016/j.celrep.2016.07.081
dc.format.number9
dc.identifier.pmcPMC5007171
dc.pubmedtypeJournal Article
dc.pubmedtypeResearch Support, N.I.H., Extramural
dc.pubmedtypeResearch Support, Non-U.S. Gov't
Appears in Collections:Fundaciones e Institutos de Investigación > IIS H. U. La Princesa > Artículos
Fundaciones e Institutos de Investigación > IIS H. U. 12 de Octubre > Artículos

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