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蛋白质乙酰化在调节线粒体融合和裂变中的作用。

The role of protein acetylation in regulating mitochondrial fusion and fission.

机构信息

Departments of Medical Genetics and Biochemistry and Molecular Biology, Alberta Children's Hospital Research Institute, Hotchkiss Brain Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.

出版信息

Biochem Soc Trans. 2021 Dec 17;49(6):2807-2819. doi: 10.1042/BST20210798.

Abstract

The dynamic processes of mitochondrial fusion and fission determine the shape of mitochondria, which can range from individual fragments to a hyperfused network, and influence mitochondrial function. Changes in mitochondrial shape can occur rapidly, allowing mitochondria to adapt to specific cues and changing cellular demands. Here, we will review what is known about how key proteins required for mitochondrial fusion and fission are regulated by their acetylation status, with acetylation promoting fission and deacetylation enhancing fusion. In particular, we will examine the roles of NAD+ dependant sirtuin deacetylases, which mediate mitochondrial acetylation, and how this post-translational modification provides an exquisite regulatory mechanism to co-ordinate mitochondrial function with metabolic demands of the cell.

摘要

线粒体融合和裂变的动态过程决定了线粒体的形状,从单个片段到超融合网络不等,并影响线粒体的功能。线粒体形状的变化可以迅速发生,使线粒体能够适应特定的信号和不断变化的细胞需求。在这里,我们将回顾一下已知的关于线粒体融合和裂变所需的关键蛋白如何通过它们的乙酰化状态来调节,其中乙酰化促进裂变,而去乙酰化增强融合。特别是,我们将研究 NAD+依赖的组蛋白去乙酰化酶在介导线粒体乙酰化中的作用,以及这种翻译后修饰如何提供一个精细的调节机制,使线粒体功能与细胞的代谢需求协调一致。

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