IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v4y2013i1d10.1038_ncomms3147.html
   My bibliography  Save this article

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

Author

Listed:
  • 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
    Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, 7-3-1 Hongo)

  • Satoshi Inoue

    (Research Center for Genomic Medicine, Saitama Medical University, 1397-1 Yamane, Hidaka-shi
    Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, 7-3-1 Hongo)

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.

Suggested Citation

  • Kazuhiro Ikeda & Sachiko Shiba & Kuniko Horie-Inoue & Kunitoshi Shimokata & Satoshi Inoue, 2013. "A stabilizing factor for mitochondrial respiratory supercomplex assembly regulates energy metabolism in muscle," Nature Communications, Nature, vol. 4(1), pages 1-9, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3147
    DOI: 10.1038/ncomms3147
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms3147
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms3147?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Ami Kobayashi & Kotaro Azuma & Toshihiko Takeiwa & Toshimori Kitami & Kuniko Horie & Kazuhiro Ikeda & Satoshi Inoue, 2023. "A FRET-based respirasome assembly screen identifies spleen tyrosine kinase as a target to improve muscle mitochondrial respiration and exercise performance in mice," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Eun-Ji Park & Hyun-Soo Kim & Do-Hyoung Lee & Su-Min Kim & Joon-Sup Yoon & Ji-Min Lee & Se Jin Im & Ho Lee & Min-Woo Lee & Chang-Woo Lee, 2023. "Ssu72 phosphatase is essential for thermogenic adaptation by regulating cytosolic translation," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3147. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.