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Direct observation of the nanoscale dynamics of membrane lipids in a living cell

Author

Listed:
  • Christian Eggeling

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Christian Ringemann

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Rebecca Medda

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Günter Schwarzmann

    (LIMES Membrane Biology and Lipid Biochemistry Unit, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany)

  • Konrad Sandhoff

    (LIMES Membrane Biology and Lipid Biochemistry Unit, University of Bonn, Gerhard-Domagk-Strasse 1, 53121 Bonn, Germany)

  • Svetlana Polyakova

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Vladimir N. Belov

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Birka Hein

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Claas von Middendorff

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Andreas Schönle

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

  • Stefan W. Hell

    (Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany)

Abstract

Nanoscale view of cell membrane lipids Cholesterol-mediated lipid interactions, such as nanodomain formation, are considered vital in a cell, but because of the lack of suitable detection techniques, their spatiotemporal range remained highly controversial. Here, Eggeling et al. use subdiffraction-resolution STED (stimulated emission depletion) fluorescence microscopy to detect the diffusion of single lipids or glycosylphosphatidylinositol (GPI)-anchored proteins on the plasma membrane of a living cell. Tuning the probing spot area up to about 70-fold below that of a confocal microscope reveals that unlike phosphoglycerolipids, sphingolipids and GPI-anchored proteins are trapped for about 10 ms in cholesterol-mediated complexes within less than 20 nm space. Optical probing in nanosized areas is a powerful new approach to study biomolecular function.

Suggested Citation

  • Christian Eggeling & Christian Ringemann & Rebecca Medda & Günter Schwarzmann & Konrad Sandhoff & Svetlana Polyakova & Vladimir N. Belov & Birka Hein & Claas von Middendorff & Andreas Schönle & Stefan, 2009. "Direct observation of the nanoscale dynamics of membrane lipids in a living cell," Nature, Nature, vol. 457(7233), pages 1159-1162, February.
    • Handle: RePEc:nat:nature:v:457:y:2009:i:7233:d:10.1038_nature07596
    DOI: 10.1038/nature07596
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    Cited by:

    1. Nario Tomishige & Maaz Nasim & Motohide Murate & Brigitte Pollet & Pascal Didier & Julien Godet & Ludovic Richert & Yasushi Sako & Yves Mély & Toshihide Kobayashi, 2023. "HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Marta Ukleja & Lara Kricks & Gabriel Torrens & Ilaria Peschiera & Ines Rodrigues-Lopes & Marcin Krupka & Julia García-Fernández & Roberto Melero & Rosa Campo & Ana Eulalio & André Mateus & María López, 2024. "Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
    3. Lucas J. Handlin & Gucan Dai, 2023. "Direct regulation of the voltage sensor of HCN channels by membrane lipid compartmentalization," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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