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Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains

Author

Listed:
  • Dragomir Milovanovic

    (Max Planck Institute for Biophysical Chemistry)

  • Alf Honigmann

    (Max Planck Institute for Biophysical Chemistry)

  • Seiichi Koike

    (Max Planck Institute for Biophysical Chemistry)

  • Fabian Göttfert

    (Max Planck Institute for Biophysical Chemistry)

  • Gesa Pähler

    (Institute for Physical Chemistry, Georg-August-University)

  • Meike Junius

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University)

  • Stefan Müllar

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University)

  • Ulf Diederichsen

    (Institute for Organic and Biomolecular Chemistry, Georg-August-University)

  • Andreas Janshoff

    (Institute for Physical Chemistry, Georg-August-University)

  • Helmut Grubmüller

    (Max Planck Institute for Biophysical Chemistry)

  • Herre J. Risselada

    (Max Planck Institute for Biophysical Chemistry
    Leibnitz Institute of Surface Modification)

  • Christian Eggeling

    (Max Planck Institute for Biophysical Chemistry
    MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, University of Oxford)

  • Stefan W. Hell

    (Max Planck Institute for Biophysical Chemistry)

  • Geert van den Bogaart

    (Max Planck Institute for Biophysical Chemistry
    Radboud University Medical Center)

  • Reinhard Jahn

    (Max Planck Institute for Biophysical Chemistry)

Abstract

The clustering of proteins and lipids in distinct microdomains is emerging as an important principle for the spatial patterning of biological membranes. Such domain formation can be the result of hydrophobic and ionic interactions with membrane lipids as well as of specific protein–protein interactions. Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismatch between the length of transmembrane domains (TMDs) and the thickness of the lipid membrane suffices to induce clustering of proteins. Even when the TMDs differ in length by only a single residue, hydrophobic mismatch can segregate structurally closely homologous membrane proteins in distinct membrane domains. Domain formation is further fine-tuned by interactions with polyanionic phosphoinositides and homo and heterotypic protein interactions. Our findings demonstrate that hydrophobic mismatch contributes to the structural organization of membranes.

Suggested Citation

  • Dragomir Milovanovic & Alf Honigmann & Seiichi Koike & Fabian Göttfert & Gesa Pähler & Meike Junius & Stefan Müllar & Ulf Diederichsen & Andreas Janshoff & Helmut Grubmüller & Herre J. Risselada & Chr, 2015. "Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains," Nature Communications, Nature, vol. 6(1), pages 1-10, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6984
    DOI: 10.1038/ncomms6984
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    Cited by:

    1. Justin A. Peruzzi & Jan Steinkühler & Timothy Q. Vu & Taylor F. Gunnels & Vivian T. Hu & Peilong Lu & David Baker & Neha P. Kamat, 2024. "Hydrophobic mismatch drives self-organization of designer proteins into synthetic membranes," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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