COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation
Mitochondrial 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 str...
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doaj-57f6b2a6d31a4e268acc95b07dda53582020-11-24T21:53:02ZengElsevierCell Reports2211-12472016-08-011692387239810.1016/j.celrep.2016.07.081COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome FormationRafael Pérez-Pérez0Teresa Lobo-Jarne1Dusanka Milenkovic2Arnaud Mourier3Ana Bratic4Alberto García-Bartolomé5Erika Fernández-Vizarra6Susana Cadenas7Aitor Delmiro8Inés García-Consuegra9Joaquín Arenas10Miguel A. Martín11Nils-Göran Larsson12Cristina Ugalde13Instituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, 50931 Cologne, GermanyDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, 50931 Cologne, GermanyDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, 50931 Cologne, GermanyInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainMedical Research Council Mitochondrial Biology Unit, CB2 0XY Cambridge, UKCentro de Biología Molecular “Severo Ochoa” (CSIC-UAM) and Departamento de Biología Molecular, Universidad Autónoma de Madrid, 28049 Madrid, SpainInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, 50931 Cologne, GermanyInstituto de Investigación, Hospital Universitario 12 de Octubre (i+12), Madrid 28041, SpainMitochondrial 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.http://www.sciencedirect.com/science/article/pii/S2211124716310270 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Rafael Pérez-Pérez Teresa Lobo-Jarne Dusanka Milenkovic Arnaud Mourier Ana Bratic Alberto García-Bartolomé Erika Fernández-Vizarra Susana Cadenas Aitor Delmiro Inés García-Consuegra Joaquín Arenas Miguel A. Martín Nils-Göran Larsson Cristina Ugalde |
spellingShingle |
Rafael Pérez-Pérez Teresa Lobo-Jarne Dusanka Milenkovic Arnaud Mourier Ana Bratic Alberto García-Bartolomé Erika Fernández-Vizarra Susana Cadenas Aitor Delmiro Inés García-Consuegra Joaquín Arenas Miguel A. Martín Nils-Göran Larsson Cristina Ugalde COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation Cell Reports |
author_facet |
Rafael Pérez-Pérez Teresa Lobo-Jarne Dusanka Milenkovic Arnaud Mourier Ana Bratic Alberto García-Bartolomé Erika Fernández-Vizarra Susana Cadenas Aitor Delmiro Inés García-Consuegra Joaquín Arenas Miguel A. Martín Nils-Göran Larsson Cristina Ugalde |
author_sort |
Rafael Pérez-Pérez |
title |
COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation |
title_short |
COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation |
title_full |
COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation |
title_fullStr |
COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation |
title_full_unstemmed |
COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation |
title_sort |
cox7a2l is a mitochondrial complex iii binding protein that stabilizes the iii2+iv supercomplex without affecting respirasome formation |
publisher |
Elsevier |
series |
Cell Reports |
issn |
2211-1247 |
publishDate |
2016-08-01 |
description |
Mitochondrial 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. |
url |
http://www.sciencedirect.com/science/article/pii/S2211124716310270 |
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