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The oxidation status of Mic19 regulates MICOS assembly.

MPS-Authors
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Jans,  D. C.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Sakowska, P., Jans, D. C., Mohanraj, K., Riedel, D., Jakobs, S., & Chacinska, A. (2015). The oxidation status of Mic19 regulates MICOS assembly. Molecular and Cellular Biology, 35(24), 4222-4237. doi:10.1128/MCB.00578-15.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0028-EDB2-0
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 cristae 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 yeast 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 proper inner membrane morphology. These findings suggest that Mic19 is a redox-dependent regulator of MICOS function.