Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1.
Dynamic regulation of mitochondrial fission through modification of the dynamin-related protein Drp1.
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DOI：
10.1111/j.1749-6632.2010.05629.x
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发表时间：
2010-07
影响因子：
5.2
通讯作者：
Blackstone C
中科院分区：
文献类型：
--
作者：
Chang CR;Blackstone C
细胞中的线粒体包括由互补的分裂和融合事件连续形成的管状囊泡网络。哺乳动物Drp1蛋白在裂变中起关键作用，而Mfn1、Mfn2和OPA1是融合所必需的。这些相反的过程之间的平衡可以迅速发生变化，表明对这些蛋白质的修饰可以调节线粒体膜动力学。我们强调线粒体分裂蛋白Drp1的翻译后修饰，这些调控机制的特点是最好的。这种动力蛋白相关的GTP酶经历了许多步骤来介导线粒体分裂，包括从细胞质易位到线粒体外膜，高阶组装成螺旋，与构象变化和膜变形相关的GTP水解，以及最终解体。这些步骤中的许多步骤可能受到Drp1的共价修饰的影响。我们讨论了动态性质的Drp1修改，以及它们如何有助于不仅正常调节线粒体分裂，而且神经病理过程。
Mitochondria in cells comprise a tubulovesicular network shaped continuously by complementary fission and fusion events. The mammalian Drp1 protein plays a key role in fission, while Mfn1, Mfn2, and OPA1 are required for fusion. Shifts in the balance between these opposing processes can occur rapidly, indicating that modifications to these proteins may regulate mitochondrial membrane dynamics. We highlight posttranslational modifications of the mitochondrial fission protein Drp1, for which these regulatory mechanisms are best characterized. This dynamin-related GTPase undergoes a number of steps to mediate mitochondrial fission, including translocation from cytoplasm to the mitochondrial outer membrane, higher-order assembly into spirals, GTP hydrolysis associated with a conformational change and membrane deformation, and ultimately disassembly. Many of these steps may be influenced by covalent modification of Drp1. We discuss the dynamic nature of Drp1 modifications and how they contribute not only to the normal regulation of mitochondrial division, but also to neuropathologic processes.
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影响因子：
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作者：
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