Autophagy regulates fatty acid availability for oxidative phosphorylation through mitochondria-endoplasmic reticulum contact sites

Claudie Bosc(Centre National de la Recherche Scientifique), Nicolas Broin(Centre National de la Recherche Scientifique), Marjorie Fanjul(Centre National de la Recherche Scientifique), Estelle Saland(Centre National de la Recherche Scientifique), Thomas Farge(Centre National de la Recherche Scientifique), Charly Courdy(Centre National de la Recherche Scientifique), Aurélie Batut, Rawand Masoud(Centre National de la Recherche Scientifique), Clément Larrue(University of Geneva), Sarah Skuli(Centre National de la Recherche Scientifique), Nicolas Espagnolle(Centre National de la Recherche Scientifique), Jean‐Christophe Pagès(Centre National de la Recherche Scientifique), Alice Carrier(Centre National de la Recherche Scientifique), Frédéric Bost(Inserm), Justine Bertrand‐Michel, Jérôme Tamburini(University of Geneva), Christian Récher(Centre National de la Recherche Scientifique), Sarah Bertoli(Centre National de la Recherche Scientifique), Véronique Mansat‐De Mas(Centre National de la Recherche Scientifique), Stéphane Manenti(Centre National de la Recherche Scientifique), Jean‐Emmanuel Sarry(Centre National de la Recherche Scientifique), Carine Joffre(Centre National de la Recherche Scientifique)
Nature Communications
August 13, 2020
Cited by 154Open Access
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Abstract

Autophagy has been associated with oncogenesis with one of its emerging key functions being its contribution to the metabolism of tumors. Therefore, deciphering the mechanisms of how autophagy supports tumor cell metabolism is essential. Here, we demonstrate that the inhibition of autophagy induces an accumulation of lipid droplets (LD) due to a decrease in fatty acid β-oxidation, that leads to a reduction of oxidative phosphorylation (OxPHOS) in acute myeloid leukemia (AML), but not in normal cells. Thus, the autophagic process participates in lipid catabolism that supports OxPHOS in AML cells. Interestingly, the inhibition of OxPHOS leads to LD accumulation with the concomitant inhibition of autophagy. Mechanistically, we show that the disruption of mitochondria-endoplasmic reticulum (ER) contact sites (MERCs) phenocopies OxPHOS inhibition. Altogether, our data establish that mitochondria, through the regulation of MERCs, controls autophagy that, in turn finely tunes lipid degradation to fuel OxPHOS supporting proliferation and growth in leukemia.


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