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Mitochondrial cristae shape regulates ROS production under restrictive glycolysis

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Corrado,  Mauro
Department Immunometabolism, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Quintana-Cabrera, R., Manjarrés-Raza, I., Vicente-Gutiérrez, C., Corrado, M., Bolaños, J. P., & Scorrano, L. (2021). Mitochondrial cristae shape regulates ROS production under restrictive glycolysis. Free Radical Biology and Medicine, 165, 18-18. doi:10.1016/j.freeradbiomed.2020.12.295.


Cite as: http://hdl.handle.net/21.11116/0000-0008-6509-D
Abstract
Mitochondrial cristae are membrane platforms where respiratory (super)complexes embed to account for oxidative phosphorylation and energy production. Despite growing evidences supporting a key role for cristae shape in determining supercomplex stability and hence respiration, it is still poorly understood whether and how the inner mitochondrial membrane links bioenergetic demands to reactive oxygen species (ROS) generation. Here we report that forced ATP fueling by mitochondria under blunted glycolysis, impacts F1FO-ATP synthase oligomerization and cristae morphology. Capitalizing on genetic and apoptotic models of cristae remodeling, we demonstrate that cristae loss and altered mitochondrial ultrastructure predispose to mitochondrial ROS generation and cell death. In this scenario, the master regulator of cristae shape Opa1 provides a scaffolding platform that prevents the collapse of cristae and mitochondrial bioenergetics, hence preventing ROS accumulation independently on changes in the cellular or mitochondrial antioxidant capacity. Both ROS generation and cell death are aggravated in conditions where the cristae scaffolding role of F1FO-ATP synthase dimers at tips or Opa1 at cristae junctions is disrupted, demonstrating that variations in mitochondrial ultrastructure are sufficient to accommodate ROS production to changes in the activity of the electron transport chain. Altogether, our results unravel a so far elusive mechanism linking bioenergetic demands and mitochondrial ultrastructure, at setting ROS levels under forced or compromised mitochondrial function.