Chojnacka Magdalena, Gornicka Agnieszka, Oeljeklaus Silke, Warscheid Bettina, Chacinska Agnieszka
From the International Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland and.
the Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg, Germany.
J Biol Chem. 2015 Jun 12;290(24):15304-12. doi: 10.1074/jbc.M115.645069. Epub 2015 Apr 27.
The mitochondrial contact site and cristae organizing system (MICOS) is a recently discovered protein complex that is crucial for establishing and maintaining the proper inner membrane architecture and contacts with the outer membrane of mitochondria. The ways in which the MICOS complex is assembled and its integrity is regulated remain elusive. Here, we report a direct link between Cox17, a protein involved in the assembly of cytochrome c oxidase, and the MICOS complex. Cox17 interacts with Mic60, thereby modulating MICOS complex integrity. This interaction does not involve Sco1, a partner of Cox17 in transferring copper ions to cytochrome c oxidase. However, the Cox17-MICOS interaction is regulated by copper ions. We propose that Cox17 is a newly identified factor involved in maintaining the architecture of the MICOS complex.
线粒体接触位点与嵴组织系统（MICOS）是最近发现的一种蛋白质复合体，对于建立和维持线粒体内膜的正常结构以及与外膜的接触至关重要。MICOS复合体的组装方式及其完整性的调控机制仍不清楚。在此，我们报告了参与细胞色素c氧化酶组装的蛋白质Cox17与MICOS复合体之间的直接联系。Cox17与Mic60相互作用，从而调节MICOS复合体的完整性。这种相互作用不涉及Cox17在将铜离子转移到细胞色素c氧化酶过程中的伙伴Sco1。然而，Cox17与MICOS的相互作用受铜离子调控。我们提出，Cox17是一个新发现的参与维持MICOS复合体结构的因子。
