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Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions

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  • Manuel Hessenberger

    (Max-Delbrück-Center for Molecular Medicine
    Institute of Biochemistry, Freie Universität Berlin)

  • Ralf M. Zerbes

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg
    Faculty of Biology, University of Freiburg)

  • Heike Rampelt

    (Institute of Biochemistry and Molecular Biology, ZBMZ, Faculty of Medicine, University of Freiburg)

  • Séverine Kunz

    (Max-Delbrück-Center for Molecular Medicine
    Core Facility Electron Microscopy, Max-Delbrück-Center for Molecular Medicine)

  • Audrey H. Xavier

    (Max-Delbrück-Center for Molecular Medicine
    Institute of Biochemistry, Freie Universität Berlin)

  • Bettina Purfürst

    (Core Facility Electron Microscopy, Max-Delbrück-Center for Molecular Medicine)

  • Hauke Lilie

    (Institute of Biochemistry and Biotechnology, Section of Protein Biochemistry, Martin Luther University Halle-Wittenberg)

  • Nikolaus Pfanner

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

  • Martin van der Laan

    (Medical Biochemistry and Molecular Biology, Center for Molecular Signaling, PZMS, Saarland University)

  • Oliver Daumke

    (Max-Delbrück-Center for Molecular Medicine
    Institute of Biochemistry, Freie Universität Berlin)

Abstract

The mitochondrial contact site and cristae organizing system (MICOS) is crucial for the formation of crista junctions and mitochondrial inner membrane architecture. MICOS contains two core components. Mic10 shows membrane-bending activity, whereas Mic60 (mitofilin) forms contact sites between inner and outer membranes. Here we report that Mic60 deforms liposomes into thin membrane tubules and thus displays membrane-shaping activity. We identify a membrane-binding site in the soluble intermembrane space-exposed part of Mic60. This membrane-binding site is formed by a predicted amphipathic helix between the conserved coiled-coil and mitofilin domains. The mitofilin domain negatively regulates the membrane-shaping activity of Mic60. Binding of Mic19 to the mitofilin domain modulates this activity. Membrane binding and shaping by the conserved Mic60–Mic19 complex is crucial for crista junction formation, mitochondrial membrane architecture and efficient respiratory activity. Mic60 thus plays a dual role by shaping inner membrane crista junctions and forming contact sites with the outer membrane.

Suggested Citation

  • Manuel Hessenberger & Ralf M. Zerbes & Heike Rampelt & Séverine Kunz & Audrey H. Xavier & Bettina Purfürst & Hauke Lilie & Nikolaus Pfanner & Martin van der Laan & Oliver Daumke, 2017. "Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions," Nature Communications, Nature, vol. 8(1), pages 1-11, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15258
    DOI: 10.1038/ncomms15258
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