PDF(Pubmed)
Abstract：
More than 99% of the mitochondrial proteome is encoded by the nucleus and requires refolding following import. Therefore, mitochondrial proteins require the coordinated action of molecular chaperones for their folding and activation. Several heat shock protein (Hsp) molecular chaperones, including members of the Hsp27, Hsp40/70, and Hsp90 families, as well as the chaperonin complex Hsp60/10 have an established role in mitochondrial protein import and folding. The \"Chaperone Code\" describes the regulation of chaperone activity by dynamic post-translational modifications; however, little is known about the post-translational regulation of mitochondrial chaperones. Dissecting the regulation of chaperone function is essential for understanding their differential regulation in pathogenic conditions and the potential development of efficacious therapeutic strategies. Here, we summarize the recent literature on post-translational regulation of mitochondrial chaperones, the consequences for mitochondrial function, and potential implications for disease.
摘要：
超过99%的线粒体蛋白质组由细胞核编码并且需要在导入后重新折叠。因此,线粒体蛋白的折叠和激活需要分子伴侣的协调作用。几种热休克蛋白(Hsp)分子伴侣,包括Hsp27、Hsp40/70和Hsp90家族的成员，Hsp60/10在线粒体蛋白导入和折叠中也有确定的作用。“伴侣代码”描述了通过动态翻译后修饰对伴侣活动的调节；但是，对线粒体伴侣的翻译后调节知之甚少。解剖伴侣功能的调节对于了解其在致病条件下的差异调节以及有效治疗策略的潜在发展至关重要。这里,我们总结了最近关于线粒体伴侣的翻译后调控的文献，对线粒体功能的影响，以及对疾病的潜在影响。
