The Oxidation Status of Mic19 Regulates MICOS Assembly |
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| Authors: | Paulina Sakowska Daniel C Jans Karthik Mohanraj Dietmar Riedel Stefan Jakobs Agnieszka Chacinska |
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| Institution: | aInternational Institute of Molecular and Cell Biology, Warsaw, Poland;bDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany;cDepartment of Neurology, University Medical Center, Göttingen, Germany;dElectron Microscopy Facility, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany |
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| Abstract: | The function of mitochondria depends on the proper organization of mitochondrial membranes. The morphology of the inner membrane is regulated by the recently identified mitochondrial contact site and crista organizing system (MICOS) complex. MICOS mutants exhibit alterations in crista formation, leading to mitochondrial dysfunction. However, the mechanisms that underlie MICOS regulation remain poorly understood. MIC19, a peripheral protein of the inner membrane and component of the MICOS complex, was previously reported to be required for the proper function of MICOS in maintaining the architecture of the inner membrane. Here, we show that human and Saccharomyces cerevisiae MIC19 proteins undergo oxidation in mitochondria and require the mitochondrial intermembrane space assembly (MIA) pathway, which couples the oxidation and import of mitochondrial intermembrane space proteins for mitochondrial localization. Detailed analyses identified yeast Mic19 in two different redox forms. The form that contains an intramolecular disulfide bond is bound to Mic60 of the MICOS complex. Mic19 oxidation is not essential for its integration into the MICOS complex but plays a role in MICOS assembly and the maintenance of the proper inner membrane morphology. These findings suggest that Mic19 is a redox-dependent regulator of MICOS function. |
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