Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation
Autor(en): | Arroum, Tasnim Borowski, Marie-Theres Marx, Nico Schmelter, Frank Scholz, Martin Psathaki, Olympia Ekaterini Hippler, Michael Enriquez, Jose Antonio Busch, Karin B. |
Stichwörter: | ARCHITECTURE; Biochemistry & Molecular Biology; complex I; MITOCHONDRIA; NDUFB10; OXPHOS; respiratory chain supercomplexes | Erscheinungsdatum: | 2023 | Herausgeber: | WALTER DE GRUYTER GMBH | Journal: | BIOLOGICAL CHEMISTRY | Volumen: | 404 | Ausgabe: | 5 | Startseite: | 399 | Seitenende: | 415 | Zusammenfassung: | The orchestrated activity of the mitochondrial respiratory or electron transport chain (ETC) and ATP synthase convert reduction power (NADH, FADH(2)) into ATP, the cell's energy currency in a process named oxidative phosphorylation (OXPHOS). Three out of the four ETC complexes are found in supramolecular assemblies: complex I, III, and IV form the respiratory supercomplexes (SC). The plasticity model suggests that SC formation is a form of adaptation to changing conditions such as energy supply, redox state, and stress. Complex I, the NADH-dehydrogenase, is part of the largest supercomplex (CI CIII2 CIVn). Here, we demonstrate the role of NDUFB10, a subunit of the membrane arm of complex I, in complex I and supercomplex assembly on the one hand and bioenergetics function on the other. NDUFB10 knockout was correlated with a decrease of SCAF1, a supercomplex assembly factor, and a reduction of respiration and mitochondrial membrane potential. This likely is due to loss of proton pumping since the CI P- P -module is downregulated and the P- D -module is completely abolished in NDUFB10 knock outs. |
ISSN: | 1431-6730 | DOI: | 10.1515/hsz-2022-0309 |
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