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. 2017 Dec 4;216(12):3917–3929. doi: 10.1083/jcb.201709172

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© 2017 Kawamata and Manfredi

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

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Figure 3. — Schematic illustration of the proposed interactions of SOD1 with mitochondrial components and their effects on OXPHOS function. SOD1 localizes to mitochondria, where it provides dismutase activity in the IMS. SOD1 is imported to the IMS via the Mia40-Erv1 disulfide relay pathway, and its maturation is facilitated by the copper chaperone for SOD1 (CCS). It is proposed that mutant misfolded SOD1 associates with various mitochondrial proteins both within the IMS and at the OM. Misfolded SOD1 interferes with the mitochondrial protein import machinery, ER–mitochondrial contacts, and VDAC. Among the electron transfer chain (ETC) complexes, mutant SOD1 mostly inhibits complex IV activity.