IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v7y2016i1d10.1038_ncomms13021.html
   My bibliography  Save this article

Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

Author

Listed:
  • Lars Ellenrieder

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    Faculty of Biology, University of Freiburg)

  • Łukasz Opaliński

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    Present address: Faculty of Biotechnology, Department of Protein Engineering, University of Wroclaw, Wroclaw 50383, Poland)

  • Lars Becker

    (School of Biology/Chemistry, University of Osnabrück)

  • Vivien Krüger

    (School of Biology/Chemistry, University of Osnabrück)

  • Oliver Mirus

    (Molecular Cell Biology of Plants, University of Frankfurt)

  • Sebastian P. Straub

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    Faculty of Biology, University of Freiburg)

  • Katharina Ebell

    (School of Biology/Chemistry, University of Osnabrück)

  • Nadine Flinner

    (Molecular Cell Biology of Plants, University of Frankfurt
    Present address: Frankfurt Institute for Advanced Studies, University of Frankfurt, Frankfurt D-60438, Germany)

  • Sebastian B. Stiller

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg)

  • Bernard Guiard

    (Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique)

  • Chris Meisinger

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signalling Studies, University of Freiburg)

  • Nils Wiedemann

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signalling Studies, University of Freiburg)

  • Enrico Schleiff

    (Molecular Cell Biology of Plants, University of Frankfurt
    Buchmann Institute of Molecular Life Sciences, Cluster of Excellence Macromolecular Complexes, University of Frankfurt)

  • Richard Wagner

    (School of Biology/Chemistry, University of Osnabrück
    Life Sciences & Chemistry, Focus Area Health, Jacobs University Bremen)

  • Nikolaus Pfanner

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signalling Studies, University of Freiburg)

  • Thomas Becker

    (Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
    BIOSS Centre for Biological Signalling Studies, University of Freiburg)

Abstract

The endoplasmic reticulum–mitochondria encounter structure (ERMES) connects the mitochondrial outer membrane with the ER. Multiple functions have been linked to ERMES, including maintenance of mitochondrial morphology, protein assembly and phospholipid homeostasis. Since the mitochondrial distribution and morphology protein Mdm10 is present in both ERMES and the mitochondrial sorting and assembly machinery (SAM), it is unknown how the ERMES functions are connected on a molecular level. Here we report that conserved surface areas on opposite sides of the Mdm10 β-barrel interact with SAM and ERMES, respectively. We generated point mutants to separate protein assembly (SAM) from morphology and phospholipid homeostasis (ERMES). Our study reveals that the β-barrel channel of Mdm10 serves different functions. Mdm10 promotes the biogenesis of α-helical and β-barrel proteins at SAM and functions as integral membrane anchor of ERMES, demonstrating that SAM-mediated protein assembly is distinct from ER-mitochondria contact sites.

Suggested Citation

  • Lars Ellenrieder & Łukasz Opaliński & Lars Becker & Vivien Krüger & Oliver Mirus & Sebastian P. Straub & Katharina Ebell & Nadine Flinner & Sebastian B. Stiller & Bernard Guiard & Chris Meisinger & Ni, 2016. "Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10," Nature Communications, Nature, vol. 7(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13021
    DOI: 10.1038/ncomms13021
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms13021
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/ncomms13021?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
    ---><---

    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:7:y:2016:i:1:d:10.1038_ncomms13021. 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.