2026-08-05T15:43:13Zhttps://repisalud.isciii.es/rest/oai/request

oai:repisalud.isciii.es:20.500.12105/107142024-09-27T09:10:27Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19605col_20.500.12105_19607

00925njm 22002777a 4500 dc Calvo, Enrique author Cogliati, Sara author Hernansanz-Agustin, Pablo author Loureiro-López, Marta author Guaras, Adela author Casuso, Rafael A. author Garcia-Marques, Fernando author Acin-Perez, Rebeca author Martí-Mateos, Yolanda author Silla-Castro, JC. author Carro-Alvarellos, Marta author Huertas, Jesús R. author Vazquez, Jesus author Enriquez, Jose Antonio author 2020-06 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. Sci Adv. 2020; 6(26):eaba7509 10.1126/sciadv.aba7509 2375-2548 Science Advances http://hdl.handle.net/20.500.12105/10714 Functional role of respiratory supercomplexes in mice: SCAF1 relevance and segmentation of the Qpool