AI Article Synopsis
- Disulfide formation in the mitochondrial intermembrane space is crucial for protein functionality and is facilitated by CHCHD4-Mia40, a key oxidoreductase and chaperone.
- Unfolded reduced proteins form a temporary complex with CHCHD4 during import; if oxidation doesn’t occur, these proteins are sent back to the cytosol for destruction.
- The study highlights a quality control mechanism for protein import that could explain issues linked to certain human disease mutants related to CHCHD4 substrates.
Article Abstract
Disulfide formation in the mitochondrial intermembrane space (IMS) is an essential process. It is catalyzed by the disulfide relay machinery, which couples substrate import and oxidation. The machinery relies on the oxidoreductase and chaperone CHCHD4-Mia40. Here, we report on the driving force for IMS import and on a redox quality control mechanism. We demonstrate that unfolded reduced proteins, upon translocation into the IMS, initiate formation of a metastable disulfide-linked complex with CHCHD4. If this interaction does not result in productive oxidation, then substrates are released to the cytosol and degraded by the proteasome. Based on these data, we propose a redox quality control step at the level of the disulfide-linked intermediate that relies on the vectorial nature of IMS import. Our findings also provide the mechanistic framework to explain failures in import of numerous human disease mutants in CHCHD4 substrates.
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| http://dx.doi.org/10.1016/j.celrep.2018.12.092 | DOI Listing |
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