Cell Biology, University of Kaiserslautern, 67663 Kaiserslautern, Germany.
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Int J Mol Sci. 2021 Sep 6;22(17):9655. doi: 10.3390/ijms22179655.
Most mitochondrial proteins are synthesized in the cytosol and targeted to the mitochondrial surface in a post-translational manner. The surface of the endoplasmic reticulum (ER) plays an active role in this targeting reaction. ER-associated chaperones interact with certain mitochondrial membrane protein precursors and transfer them onto receptor proteins of the mitochondrial surface in a process termed ER-SURF. ATP-driven proteins in the membranes of mitochondria (Msp1, ATAD1) and the ER (Spf1, P5A-ATPase) serve as extractors for the removal of mislocalized proteins. If the re-routing to mitochondria fails, precursors can be degraded by ER or mitochondria-associated degradation (ERAD or MAD respectively) in a proteasome-mediated reaction. This review summarizes the current knowledge about the cooperation of the ER and mitochondria in the targeting and quality control of mitochondrial precursor proteins.
大多数线粒体蛋白是在细胞质中合成的，然后以翻译后修饰的方式靶向到线粒体表面。内质网（ER）的表面在这个靶向反应中起着积极的作用。ER 相关伴侣与某些线粒体膜蛋白前体相互作用，并将它们转移到线粒体表面的受体蛋白上，这个过程称为 ER-SURF。线粒体膜中的 ATP 驱动蛋白（Msp1、ATAD1）和 ER（Spf1、P5A-ATPase）作为提取器，用于去除定位错误的蛋白质。如果重新路由到线粒体失败，前体可以通过 ER 或线粒体相关降解（分别为 ERAD 或 MAD）在蛋白酶体介导的反应中被降解。这篇综述总结了 ER 和线粒体在靶向和线粒体前体蛋白质量控制中的合作的最新知识。
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