Journal
SCIENCE ADVANCES
Volume 6, Issue 26, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aba7509
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Funding
- MINECO [SAF2015-65633-R]
- MCIU [RTI2018-099357-B-I00]
- CIBERFES [CB16/10/00282]
- HFSP [RGP0016/2018]
- ISCIII-SGEFI/FEDER, ProteoRed [ISCIII-IPT13/0001]
- Fundacio MaratoTV3 [122/C/2015]
- la Caixa Banking Foundation [HR17-00247]
- Ministry of Economy, Industry and Competitiveness (MEIC)
- Pro-CNIC Foundation
- MINECO award [SEV-2015-0505]
- [MINECO-BIO2015-67580-P]
- [PGC2018-097019-B-I00]
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Mitochondrial respiratory complexes assemble into supercomplexes (SC). Q-respirasome (III2 + IV) requires the supercomplex assembly factor (SCAF1) protein. The role of this factor in the N-respirasome (I + III2 + IV) and the physiological role of SCs are controversial. Here, we study C57BL/6J mice harboring nonfunctional SCAF1, the full knockout for SCAF1, or the wild-type version of the protein and found that exercise performance is SCAF1 dependent. By combining quantitative data-independent proteomics, 2D Blue native gel electrophoresis, and functional analysis of enriched respirasome fractions, we show that SCAF1 confers structural attachment between III2 and IV within the N-respirasome, increases NADH-dependent respiration, and reduces reactive oxygen species (ROS). Furthermore, the expression of AOX in cells and mice confirms that CI-CIII superassembly segments the CoQ in two pools and modulates CI-NADH oxidative capacity.
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