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

Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS.
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肌球蛋白 19 产生的机械不稳定性有助于线粒体嵴结构和 OXPHOS

DOI:
10.1038/s41467-022-30431-3
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发表时间:
2022-05-13
影响因子:
16.6
通讯作者:
--
中科院分区:
综合性期刊1区
文献类型:
--
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折叠的线粒体内膜嵴是氧化磷酸化(OXPHOS)和能量产生的结构基础。通过机械模拟线粒体形态发生,我们推测,有效的雕刻嵴是细胞器的非自治。长久以来,人们一直认为生命系统的折叠需要屈曲。然而,尚未确定嵴形成和调节的束缚力。结合电子断层扫描,蛋白质组学策略,超分辨率活细胞成像和数学建模,我们揭示了线粒体定位的肌动蛋白马达肌球蛋白19(Myo 19)是维持嵴结构的关键,通过与SAM-MICOS超复合物。我们发现Myo 19的耗竭或其运动活性的破坏导致线粒体膜电位改变和OXPHOS减少。我们建议,Myo 19可以作为一个机械系绳有效脊线粒体嵴,从而维持各种细胞功能所必需的能量稳态。
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.
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