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COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation.

MPG-Autoren

Pérez-Pérez,  Rafael
Max Planck Institute for Biology of Ageing, Max Planck Society;

Lobo-Jarne,  Teresa
Max Planck Institute for Biology of Ageing, Max Planck Society;

Milenkovic,  Dusanka
Max Planck Institute for Biology of Ageing, Max Planck Society;

Mourier,  Arnaud
Max Planck Institute for Biology of Ageing, Max Planck Society;

Bratic,  Ana
Max Planck Institute for Biology of Ageing, Max Planck Society;

García-Bartolomé,  Alberto
Max Planck Institute for Biology of Ageing, Max Planck Society;

Fernández-Vizarra,  Erika
Max Planck Institute for Biology of Ageing, Max Planck Society;

Cadenas,  Susana
Max Planck Institute for Biology of Ageing, Max Planck Society;

Delmiro,  Aitor
Max Planck Institute for Biology of Ageing, Max Planck Society;

García-Consuegra,  Inés
Max Planck Institute for Biology of Ageing, Max Planck Society;

Arenas,  Joaquín
Max Planck Institute for Biology of Ageing, Max Planck Society;

Martín,  Miguel A
Max Planck Institute for Biology of Ageing, Max Planck Society;

Larsson,  Nils-Göran
Max Planck Institute for Biology of Ageing, Max Planck Society;

Ugalde,  Cristina
Max Planck Institute for Biology of Ageing, Max Planck Society;

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Zitation

Pérez-Pérez, R., Lobo-Jarne, T., Milenkovic, D., Mourier, A., Bratic, A., García-Bartolomé, A., et al. (2016). COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation. Cell reports, 16(9), 2387-2398. doi:10.1016/j.celrep.2016.07.081.


Zusammenfassung
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.