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

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 () and Congying Wu ()
Additional contact information
Peng Shi: School of Basic Medical Sciences, Peking University Health Science Center
Xiaoyu Ren: School of Basic Medical Sciences, Peking University Health Science Center
Jie Meng: Tsinghua University
Chenlu Kang: School of Basic Medical Sciences, Peking University Health Science Center
Yihe Wu: School of Basic Medical Sciences, Peking University Health Science Center
Yingxue Rong: School of Basic Medical Sciences, Peking University Health Science Center
Shujuan Zhao: Peking University
Zhaodi Jiang: National Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University
Ling Liang: Peking University Health Science Center
Wanzhong He: National Institute of Biological Sciences, Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University
Yuxin Yin: School of Basic Medical Sciences, Peking University Health Science Center
Xiangdong Li: Chinese Academy of Sciences
Yong Liu: Xuzhou Medical University
Xiaoshuai Huang: Peking University
Yujie Sun: Peking University
Bo Li: Tsinghua University
Congying Wu: School of Basic Medical Sciences, Peking University Health Science Center

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-30431-3

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