Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2023 Mar 24;404(5):399-415.
doi: 10.1515/hsz-2022-0309. Print 2023 Apr 25.

Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation

Tasnim Arroum  1 , Marie-Theres Borowski  1 , Nico Marx  1 , Frank Schmelter  1 , Martin Scholz  2 , Olympia Ekaterini Psathaki  3 , Michael Hippler  2 , José Antonio Enriquez  4   5 , Karin B Busch  1
Affiliations
Free article

Loss of respiratory complex I subunit NDUFB10 affects complex I assembly and supercomplex formation

Tasnim Arroum et al. Biol Chem. .
Free article

Abstract

The orchestrated activity of the mitochondrial respiratory or electron transport chain (ETC) and ATP synthase convert reduction power (NADH, FADH2) 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.

Keywords: NDUFB10; OXPHOS; complex I; mitochondria; respiratory chain supercomplexes.

PubMed Disclaimer

References

    1. Acin-Perez, R. and Enriquez, J.A. (2014). The function of the respiratory supercomplexes: the plasticity model. Biochim. Biophys. Acta 1837: 444–450, https://doi.org/10.1016/j.bbabio.2013.12.009 . - DOI
    1. Acin-Perez, R., Fernandez-Silva, P., Peleato, M.L., Perez-Martos, A., and Enriquez, J.A. (2008). Respiratory active mitochondrial supercomplexes. Mol. Cell. 32: 529–539, https://doi.org/10.1016/j.molcel.2008.10.021 . - DOI
    1. Barrientos, A. and Ugalde, C. (2013). I function, therefore I am: overcoming skepticism about mitochondrial supercomplexes. Cell Metabol. 18: 147–149, https://doi.org/10.1016/j.cmet.2013.07.010 . - DOI
    1. Blaza, J.N., Serreli, R., Jones, A.J., Mohammed, K., and Hirst, J. (2014). Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes. Proc. Natl. Acad. Sci. U.S.A. 111: 15735–15740, https://doi.org/10.1073/pnas.1413855111 . - DOI
    1. Brandt, U. (2006). Energy converting NADH: quinone oxidoreductase (complex I). Annu. Rev. Biochem. 75: 69–92, https://doi.org/10.1146/annurev.biochem.75.103004.142539 . - DOI

Publication types

MeSH terms

LinkOut - more resources