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GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane

Author

Listed:
  • Eva Sevcsik

    (Institute of Applied Physics, Vienna University of Technology)

  • Mario Brameshuber

    (Institute of Applied Physics, Vienna University of Technology)

  • Martin Fölser

    (Institute of Applied Physics, Vienna University of Technology)

  • Julian Weghuber

    (School of Engineering and Environmental Sciences, University of Applied Sciences Upper Austria)

  • Alf Honigmann

    (Max-Planck-Institute for Biophysical Chemistry
    Present address: Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstr. 108, Dresden 01307, Germany)

  • Gerhard J. Schütz

    (Institute of Applied Physics, Vienna University of Technology)

Abstract

The organization of proteins and lipids in the plasma membrane has been the subject of a long-lasting debate. Membrane rafts of higher lipid chain order were proposed to mediate protein interactions, but have thus far not been directly observed. Here we use protein micropatterning combined with single-molecule tracking to put current models to the test: we rearranged lipid-anchored raft proteins (glycosylphosphatidylinositol(GPI)-anchored-mGFP) directly in the live cell plasma membrane and measured the effect on the local membrane environment. Intriguingly, this treatment does neither nucleate the formation of an ordered membrane phase nor result in any enrichment of nanoscopic-ordered domains within the micropatterned regions. In contrast, we find that immobilized mGFP-GPIs behave as inert obstacles to the diffusion of other membrane constituents without influencing their membrane environment over distances beyond their physical size. Our results indicate that phase partitioning is not a fundamental element of protein organization in the plasma membrane.

Suggested Citation

  • Eva Sevcsik & Mario Brameshuber & Martin Fölser & Julian Weghuber & Alf Honigmann & Gerhard J. Schütz, 2015. "GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7969
    DOI: 10.1038/ncomms7969
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