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- W2888505982 abstract "Abstract It is unclear how the mitochondrial fusion protein Optic atrophy 1 (OPA1), which inhibits cristae remodeling, protects from mitochondrial dysfunction. Here we identify the mitochondrial F 1 F o -ATP synthase as the effector of OPA1 in mitochondrial protection. In OPA1 overexpressing cells, the loss of proton electrochemical gradient caused by respiratory chain complex III inhibition is blunted and this protection is abolished by the ATP synthase inhibitor oligomycin. Mechanistically, OPA1 and ATP synthase can interact, but recombinant OPA1 fails to promote oligomerization of purified ATP synthase reconstituted in liposomes, suggesting that OPA1 favors ATP synthase oligomerization and reversal activity by modulating cristae shape. When ATP synthase oligomers are genetically destabilized by silencing the key dimerization subunit e , OPA1 is no longer able to preserve mitochondrial function and cell viability upon complex III inhibition. Thus, OPA1 protects mitochondria from respiratory chain inhibition by stabilizing cristae shape and favoring ATP synthase oligomerization." @default.
- W2888505982 created "2018-08-31" @default.
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- W2888505982 date "2018-08-24" @default.
- W2888505982 modified "2023-10-17" @default.
- W2888505982 title "The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function" @default.
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- W2888505982 doi "https://doi.org/10.1038/s41467-018-05655-x" @default.
- W2888505982 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6109181" @default.
- W2888505982 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30143614" @default.
- W2888505982 hasPublicationYear "2018" @default.
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