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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F24%3A00598238" target="_blank" >RIV/67985823:_____/24:00598238 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/24:00598238 RIV/00216208:11310/24:10486380 RIV/00064165:_____/24:10486380 RIV/00216208:11110/24:10486380

Výsledek na webu

<a href="https://doi.org/10.1016/j.isci.2024.110560" target="_blank" >https://doi.org/10.1016/j.isci.2024.110560</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.isci.2024.110560" target="_blank" >10.1016/j.isci.2024.110560</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

30202 - Endocrinology and metabolism (including diabetes, hormones)

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

iScience

ISSN

2589-0042

e-ISSN

2589-0042

Svazek periodika

27

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

22

Strana od-do

110560

Kód UT WoS článku

001285662900001

EID výsledku v databázi Scopus

2-s2.0-85199960580