Cdc48 AAA ATPase Regulates Protein Dynamics and Turnover in Mitochondria
Cdc48 AAA ATPase Regulates Protein Dynamics and Turnover in Mitochondria
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DOI：
10.1016/b978-0-12-812146-7.00005-6
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发表时间：
2017-01-01
期刊：
影响因子：
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通讯作者：
Esaki, Masatoshi
中科院分区：
文献类型：
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作者：
Esaki, Masatoshi
蛋白质降解不仅有助于去除异常蛋白质，而且有助于调节生物反应。AAA ATP酶Cdc48和蛋白酶体广泛参与细胞质中的蛋白质降解。Cdc48和蛋白酶体还调节线粒体外膜蛋白质的质量控制，包括抗凋亡因子和负责融合事件期间线粒体外膜系留的丝裂融合蛋白。Cdc48的ATP酶缺陷突变体抑制线粒体融合，并且已经提出线粒体膜融合的进展需要线粒体融合素降解。相反，最近的证据表明，Cdc48可能介导线粒体融合的线粒体融合蛋白拴系复合物的解体。因此，胞质AAA蛋白不仅通过调节蛋白质稳定性，而且通过调节复合物形成来控制线粒体完整性。本文综述了Cdc48如何调控线粒体蛋白质的质量和形态。
Protein degradation contributes to not only the removal of abnormal proteins but also the regulation of biological reactions. The AAA ATPase Cdc48 and the proteasome are widely involved in protein degradation in the cytosol. Cdc48 and the proteasome also regulate quality control of mitochondrial outer membrane proteins including antiapoptotic factors and mitofusins that are responsible for tethering of the mitochondrial outer membrane during fusion events. ATPase-deficient mutants of Cdc48 inhibit mitochondrial fusion and collectively, it has been proposed that mitofusin degradation is required for the progression of mitochondrial membrane fusion. In contrast, recent evidence suggests that Cdc48 may mediate mitochondrial fusion by disassembly of mitofusin tethering complexes. The cytosolic AAA protein thus controls mitochondrial integrity by regulating not only protein stability but also complex formation. This review provides a detailed exploration of how Cdc48 functions to regulate mitochondrial protein quality and morphology.