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A stabilizing factor for mitochondrial respiratory supercomplex assembly regulates energy metabolism in muscle

Kazuhiro Ikeda, Sachiko Shiba, Kuniko Horie-Inoue, Kunitoshi Shimokata and Satoshi Inoue ()
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Kazuhiro Ikeda: Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi
Sachiko Shiba: Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi
Kuniko Horie-Inoue: Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi
Kunitoshi Shimokata: Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi
Satoshi Inoue: Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi

Nature Communications, 2013, vol. 4, issue 1, 1-9

Abstract: Abstract The mitochondrial respiratory chain is essential for oxidative phosphorylation and comprises multiple complexes, including cytochrome c oxidase, assembled in macromolecular supercomplexes. Little is known about factors that contribute to supercomplex organization. Here we identify COX7RP as a factor that promotes supercomplex assembly. Cox7rp-knockout mice exhibit decreased muscular activity and heat production failure in the cold due to reduced COX activity. In contrast, COX7RP-transgenic mice exhibit increased exercise performance with increased cytochrome c oxidase activity. Two-dimensional blue native electrophoresis reveals that COX7RP is a key molecule that promotes assembly of the III2/IVn supercomplex with complex I. Our study identified COX7RP as a protein that functions in I/III2/IVn supercomplex assembly and is required for full activity of mitochondrial respiration.

Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3147

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DOI: 10.1038/ncomms3147

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