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. 2024 Oct 17;7:1342. doi: 10.1038/s42003-024-07042-3

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 8 — a, b Muscle mitochondria from PK2 KtoA mutants have increased complex I and decreased complex II basal respiration and each cannot be uncoupled. a Complex I (glutamate and malate) stimulated basal and uncoupled mitochondrial oxygen consumption rates measured in isolated muscle mitochondria from wild type (wt), unc-89(sf22), and unc-89 (syb1360) mutant strains (n = 3–8 per strain). b Complex II (succinate) stimulated basal and uncoupled mitochondrial oxygen consumption rates measured in isolated muscle mitochondria from wild type (wt), unc-89(sf22), and unc-89 (syb1360) mutant strains (n = 4–5 per strain). Means and standard errors of the mean are represented. Significance was tested by one-way ANOVA followed by Tukey’s post hoc test. *p ≤ 0.05, **p ≤ 0.005, ***p ≤ 0.0005, ****p ≤ 0.00005. c, d PK2 KtoA mutants have altered levels of electron transport chain complexes. c Representative western blots reacted against antibodies to the indicated components of complexes I, II, IV, V, and cytochrome C. d Quantitation of these results with n = 3. au: arbitrary units. Statistical significance was assessed using an unpaired t-test with Welch’s correction. Note that as compared to wild type, complexes I and V are normal, but complexes II and IV are reduced, and cytochrome C is elevated in the PK2 KtoA mutants.