Journal article
The assembly factor SDHAF2 is dispensable for flavination of the catalytic subunit of mitochondrial complex II in breast cancer cells
A Bezawork-Geleta, L Dong, J Rohlena, J Neuzil
Journal of Biological Chemistry | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 2016
Abstract
Mitochondrial complex II or succinate dehydrogenase (SDH) is at the crossroads of oxidative phosphorylation and the tricarboxylic acid cycle. It has been shown that Sdh5 (SDHAF2/SDH5 in mammals) is required for flavination of the subunit Sdh1 (SDHA in human cells) in yeast. Here we demonstrate that in human breast cancer cells, SDHAF2/SDH5 is dispensable for SDHA flavination. In contrast to yeast, CRISPR-Cas9 nickase-mediated SDHAF2 KO breast cancer cells feature flavinated SDHA and retain fully assembled and functional complex II, as well as normal mitochondrial respiration. Our data show that SDHA flavination is independent of SDHAF2 in breast cancer cells, employing an alternative mechani..
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Awarded by Australian Research Council
Funding Acknowledgements
This work was supported by a grant from the Australian Research Council, a Griffith University New Researcher grant, Czech Research Foundation Grants 15-02203S and 16-22823S, and funding from BIOCEV (Grant CZ.1.05/1.1.00/02.0109). The authors declare that they have no conflicts of interest with the contents of this article.