Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS.

Nature communications 2022 May 13

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The folded mitochondria inner membrane-cristae is the structural foundation for oxidative phosphorylation (OXPHOS) and energy production. By mechanically simulating mitochondria morphogenesis, we speculate that efficient sculpting of the cristae is organelle non-autonomous. It has long been inferred that folding requires buckling in living systems. However, the tethering force for cristae formation and regulation has not been identified. Combining electron tomography, proteomics strategies, super resolution live cell imaging and mathematical modeling, we reveal that the mitochondria localized actin motor-myosin 19 (Myo19) is critical for maintaining cristae structure, by associating with the SAM-MICOS super complex. We discover that depletion of Myo19 or disruption of its motor activity leads to altered mitochondria membrane potential and decreased OXPHOS. We propose that Myo19 may act as a mechanical tether for effective ridging of the mitochondria cristae, thus sustaining the energy homeostasis essential for various cellular functions. © 2022. The Author(s).

Citation

Peng Shi, Xiaoyu Ren, Jie Meng, Chenlu Kang, Yihe Wu, Yingxue Rong, Shujuan Zhao, Zhaodi Jiang, Ling Liang, Wanzhong He, Yuxin Yin, Xiangdong Li, Yong Liu, Xiaoshuai Huang, Yujie Sun, Bo Li, Congying Wu. Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS. Nature communications. 2022 May 13;13(1):2673