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. 2022 Feb 16;13(2):156. doi: 10.1038/s41419-022-04602-5

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© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — A Immunoblot of OMA1 KO, Yme1L KO, OMA1 Yme1L DKO, and WT HeLa cells treated with dimethyl sulfoxide (DMSO) or 10 μm Oligomycin for 8 h. GAPDH served as loading controls. B Immunoblot of WT and CHCHD2 KO HeLa cell lines which stably express CHCHD2 WT, T61I or R145Q mutation where indicated, treated with either vehicle or 125 μm Oligomycin for 6 h. GAPDH served as the loading control. C Quantification of levels CHCHD2 and its mutation CHCHD2-T61I and CHCHD2-R145Q from B. The relative protein levels were evaluated by densitometry analysis using ImageJ software and were quantified for the ratio of CHCHD2/GAPDH, T61I /GAPDH, and R145Q/GAPDH (n = 3 independent experiments). The data are presented as mean ± SD.