Stress-induced hyperacetylation of microtubule enhances mitochondrial fission and modulates the phosphorylation of Drpl at 616Ser
Stress-induced hyperacetylation of microtubule enhances mitochondrial fission and modulates the phosphorylation of Drpl at 616Ser
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DOI：
10.1016/j.cellsig.2017.07.020
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发表时间：
2017-11-01
影响因子：
4.8
通讯作者：
Pous, Christian
中科院分区：
文献类型：
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作者：
Perdiz, Daniel;Lorin, Severine;Pous, Christian
线粒体动力学是由分裂和融合事件造成的，这些事件可能是不平衡的，有利于细胞应激时线粒体的碎裂。在氧化应激过程中，微管以线粒体依赖的方式过度乙酰化。在这项研究中，我们发现在应激条件下，大多数线粒体形成带有携带DRp1的微管结构域的焦点。我们还证明，压力诱导的微管超乙酰化是有效诱导DRp1在(616)Ser处磷酸化所必需的，这是一种依赖于kinesin-1和c-jun N末端激酶的方式。此外，微管的高乙酰化有助于将总的Drp1募集到线粒体以促进分裂。这些结果突出了微管和线粒体动力学之间相互作用的一种新方式。
Mitochondria dynamics results from fission and fusion events that may be unbalanced in favor of mitochondrial fragmentation upon cell stress. During oxidative stress, microtubules are hyperacetylated in a mitochondria dependent manner. In this study, we show that under stress conditions, most of the mitochondria form foci with microtubule domains that carry Drp1. We also demonstrate that stress-induced hyperacetylation of microtubules is required for the effective induction of Drp1 phosphorylation at (616)Ser, in a kinesin-1- and c-Jun N-terminal kinase-dependent manner. Furthermore, hyperacetylation of microtubules contributes to the recruitment of total Drp1 to mitochondria to enhance fission. These results highlight a new way of interaction between microtubules and mitochondria dynamics.