Mitochondrial Contact Site and Cristae Organization System and F1FO-ATP Synthase Crosstalk Is a Fundamental Property of Mitochondrial Cristae (vol 6, e00327-21, 2021)

0557503 - BC 2022 RIV US eng O - Others
Cadena, Lawrence Rudy - Gahura, Ondřej - Panicucci, Brian - Zíková, Alena - Hashimi, Hassan
Mitochondrial Contact Site and Cristae Organization System and F1FO-ATP Synthase Crosstalk Is a Fundamental Property of Mitochondrial Cristae (vol 6, e00327-21, 2021).
2022. mSphere. American Society for Microbiology. Roč. 6, č. 3 (2022), č. článku e00327-21. ISSN 2379-5042. E-ISSN 2379-5042
R&D Projects: GA ČR(CZ) GA20-23513S; GA ČR(CZ) GA18-17529S; GA MŠMT(CZ) EF16_019/0000759; GA MŠMT(CZ) LM2015062; GA ČR(CZ) GJ20-04150Y
Institutional support: RVO:60077344
Keywords : atp synthase * organizing system * f1f0-atp synthase
OECD category: Cell biology
https://journals.asm.org/doi/epub/10.1128/msphere.00189-22

Mitochondrial cristae are polymorphic invaginations of the inner membrane that are the fabric of cellular respiration. Both the mitochondrial contact site and cristae organization system (MICOS) and the F1FO-ATP synthase are vital for sculpting cristae by opposing membrane-bending forces. While MICOS promotes negative curvature at crista junctions, dimeric F1FO-ATP synthase is crucial for positive curvature at crista rims. Crosstalk between these two complexes has been observed in baker's yeast, the model organism of the Opisthokonta supergroup. Here, we report that this property is con-served in Trypanosoma brucei, a member of the Discoba clade that separated from the Opisthokonta similar to 2 billion years ago. Specifically, one of the paralogs of the core MICOS subunit Mic10 interacts with dimeric F1FO-ATP synthase, whereas the other core Mic60 subunit has a counteractive effect on F1FO-ATP synthase oligomerization. This is evoca-tive of the nature of MICOS-F1FO-ATP synthase crosstalk in yeast, which is remarkable given the diversification that these two complexes have undergone during almost 2 eons of independent evolution. Furthermore, we identified a highly diverged, putative homolog of subunit e, which is essential for the stability of F1FO-ATP synthase dimers in yeast. Just like subunit e, it is preferentially associated with dimers and interacts with Mic10, and its silencing results in severe defects to cristae and the disintegration of F1FO-ATP synthase dimers. Our findings indicate that crosstalk between MICOS and dimeric F1FO-ATP synthase is a fundamental property impacting crista shape throughout eukaryotes.
Permanent Link: https://hdl.handle.net/11104/0333086