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Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact

Author

Listed:
  • Nadav Shai

    (Weizmann Institute of Science)

  • Eden Yifrach

    (Weizmann Institute of Science)

  • Carlo W. T. Roermund

    (University of Amsterdam)

  • Nir Cohen

    (Weizmann Institute of Science)

  • Chen Bibi

    (Weizmann Institute of Science)

  • Lodewijk IJlst

    (University of Amsterdam)

  • Laetitia Cavellini

    (Institut de Biologie Physico-Chimique, Sorbonne Universités)

  • Julie Meurisse

    (Institut de Biologie Physico-Chimique, Sorbonne Universités)

  • Ramona Schuster

    (University of Cologne)

  • Lior Zada

    (Weizmann Institute of Science)

  • Muriel C. Mari

    (University of Groningen, University Medical Center Groningen)

  • Fulvio M. Reggiori

    (University of Groningen, University Medical Center Groningen)

  • Adam L. Hughes

    (University of Utah School of Medicine)

  • Mafalda Escobar-Henriques

    (University of Cologne)

  • Mickael M. Cohen

    (Institut de Biologie Physico-Chimique, Sorbonne Universités)

  • Hans R. Waterham

    (University of Amsterdam)

  • Ronald J. A. Wanders

    (University of Amsterdam)

  • Maya Schuldiner

    (Weizmann Institute of Science)

  • Einat Zalckvar

    (Weizmann Institute of Science)

Abstract

The understanding that organelles are not floating in the cytosol, but rather held in an organized yet dynamic interplay through membrane contact sites, is altering the way we grasp cell biological phenomena. However, we still have not identified the entire repertoire of contact sites, their tethering molecules and functions. To systematically characterize contact sites and their tethering molecules here we employ a proximity detection method based on split fluorophores and discover four potential new yeast contact sites. We then focus on a little-studied yet highly disease-relevant contact, the Peroxisome-Mitochondria (PerMit) proximity, and uncover and characterize two tether proteins: Fzo1 and Pex34. We genetically expand the PerMit contact site and demonstrate a physiological function in β-oxidation of fatty acids. Our work showcases how systematic analysis of contact site machinery and functions can deepen our understanding of these structures in health and disease.

Suggested Citation

  • Nadav Shai & Eden Yifrach & Carlo W. T. Roermund & Nir Cohen & Chen Bibi & Lodewijk IJlst & Laetitia Cavellini & Julie Meurisse & Ramona Schuster & Lior Zada & Muriel C. Mari & Fulvio M. Reggiori & Ad, 2018. "Systematic mapping of contact sites reveals tethers and a function for the peroxisome-mitochondria contact," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03957-8
    DOI: 10.1038/s41467-018-03957-8
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