0598238 - FGÚ 2025 RIV US eng J - Journal Article
Čunátová, Kristýna - Vrbacký, Marek - Puertas-Frias, Guillermo - Alán, Lukáš - Vanišová, M. - Saucedo-Rodríguez, María José - Houštěk, Josef - Fernández-Vizarra, E. - Neužil, Jiří - Pecinová, Alena - Pecina, Petr - Mráček, Tomáš
Mitochondrial translation is the primary determinant of secondary mitochondrial complex I deficiencies.
iScience. Roč. 27, č. 8 (2024), č. článku 110560. E-ISSN 2589-0042
R&D Projects: GA MŠMT(CZ) EF18_046/0016045; GA ČR(CZ) GA21-18993S; GA ČR(CZ) GA22-21082S; GA MŠMT(CZ) LX22NPO5104; GA MZd(CZ) NU22-01-00499
Research Infrastructure: Czech-BioImaging III - 90250
Institutional support: RVO:67985823 ; RVO:86652036 ; RVO:68378050
Keywords : oxidative phosphorylation system (OXPHOS) * ATP synthase * biogenesis * mitochondria
OECD category: Endocrinology and metabolism (including diabetes, hormones); Endocrinology and metabolism (including diabetes, hormones) (BTO-N)
Impact factor: 4.6, year: 2023 ; AIS: 1.5, rok: 2023
Method of publishing: Open access
Result website:
https://doi.org/10.1016/j.isci.2024.110560DOI: https://doi.org/10.1016/j.isci.2024.110560

Individual complexes of the mitochondrial oxidative phosphorylation system (OXPHOS) are not linked solely by their function, they also share dependencies at the maintenance/assembly level, where one complex depends on the presence of a different individual complex. Despite the relevance of this “interdependence” behavior for mitochondrial diseases, its true nature remains elusive. To understand the mechanism that can explain this phenomenon, we examined the consequences of the aberration of different OXPHOS complexes in human cells. We demonstrate here that the complete disruption of each of the OXPHOS complexes resulted in a decrease in the complex I (cI) level and that the major reason for this is linked to the downregulation of mitochondrial ribosomal proteins. We conclude that the secondary cI defect is due to mitochondrial protein synthesis attenuation, while the responsible signaling pathways could differ based on the origin of the OXPHOS defect.
Permanent Link: https://hdl.handle.net/11104/0355965