Mitochondrial translation is the primary determinant of secondary mitochondrial complex I deficiencies

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

doi:https://dx.doi.org/10.1016/j.bbabio.2024.149424

Number of the records: 1

Mitochondrial translation is the primary determinant of secondary mitochondrial complex I deficiencies

1.

SYSNO ASEP	0600275
Document Type	A - Abstract
R&D Document Type	O - Ostatní
Title	Mitochondrial translation is the primary determinant of secondary mitochondrial complex I deficiencies
Author(s)	Čunátová, Kristýna (FGU-C)_{RID, ORCID} Vrbacký, Marek (FGU-C)_{RID, ORCID} Puertas-Frias, Guillermo (FGU-C)_{RID, ORCID} Alán, Lukáš (FGU-C)_{RID, ORCID} Vanišová, M. (CZ) Saucedo-Rodríguez, María José (FGU-C)_RID Houštěk, Josef (FGU-C)_{RID, ORCID} Fernández-Vizarra, E. (IT) Neužil, Jiří (BTO-N)_{RID, ORCID} Pecinová, Alena (FGU-C)_{RID, ORCID, SAI} Pecina, Petr (FGU-C)_{RID, ORCID} Mráček, Tomáš (FGU-C)_{RID, ORCID}
Source Title	Biochimica Et Biophysica Acta-Bioenergetics. - : Elsevier - ISSN 0005-2728 Roč. 1865, Suppl.1 (2024), s. 119-120
Number of pages	1 s.
Action	European Bioenergetics Conference /22./
Event date	26.08.2024 - 31.08.2024
VEvent location	Innsbruck
Country	AT - Austria
Event type	EUR
Language	eng - English
Country	NL - Netherlands
Keywords	oxidative phosphorylation system (OXPHOS) ; ATP synthase ; biogenesis ; mitochondria
OECD category	Endocrinology and metabolism (including diabetes, hormones)
R&D Projects	LX22NPO5104 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
Institutional support	FGU-C - RVO:67985823 ; BTO-N - RVO:86652036
UT WOS	001311206700318
DOI	https://doi.org/10.1016/j.bbabio.2024.149424
Annotation	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.
Workplace	Institute of Physiology
Contact	Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
Year of Publishing	2025
Electronic address	https://doi.org/10.1016/j.bbabio.2024.149424

Number of the records: 1