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Multi-protein assemblies underlie the mesoscale organization of the plasma membrane

Author

Listed:
  • Sinem K. Saka

    (University of Göttingen Medical Centre, and Centre for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB)
    International Max Planck Research School Molecular Biology)

  • Alf Honigmann

    (Max Planck Institute for Biophysical Chemistry)

  • Christian Eggeling

    (MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine)

  • Stefan W. Hell

    (Max Planck Institute for Biophysical Chemistry)

  • Thorsten Lang

    (Life and Medical Sciences (LIMES) Institute, University of Bonn)

  • Silvio O. Rizzoli

    (University of Göttingen Medical Centre, and Centre for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB))

Abstract

Most proteins have uneven distributions in the plasma membrane. Broadly speaking, this may be caused by mechanisms specific to each protein, or may be a consequence of a general pattern that affects the distribution of all membrane proteins. The latter hypothesis has been difficult to test in the past. Here, we introduce several approaches based on click chemistry, through which we study the distribution of membrane proteins in living cells, as well as in membrane sheets. We found that the plasma membrane proteins form multi-protein assemblies that are long lived (minutes), and in which protein diffusion is restricted. The formation of the assemblies is dependent on cholesterol. They are separated and anchored by the actin cytoskeleton. Specific proteins are preferentially located in different regions of the assemblies, from their cores to their edges. We conclude that the assemblies constitute a basic mesoscale feature of the membrane, which affects the patterning of most membrane proteins, and possibly also their activity.

Suggested Citation

  • Sinem K. Saka & Alf Honigmann & Christian Eggeling & Stefan W. Hell & Thorsten Lang & Silvio O. Rizzoli, 2014. "Multi-protein assemblies underlie the mesoscale organization of the plasma membrane," Nature Communications, Nature, vol. 5(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5509
    DOI: 10.1038/ncomms5509
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    Cited by:

    1. Ling-Gang Wu & Chung Yu Chan, 2024. "Membrane transformations of fusion and budding," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Tal M. Dankovich & Rahul Kaushik & Linda H. M. Olsthoorn & Gabriel Cassinelli Petersen & Philipp Emanuel Giro & Verena Kluever & Paola Agüi-Gonzalez & Katharina Grewe & Guobin Bao & Sabine Beuermann &, 2021. "Extracellular matrix remodeling through endocytosis and resurfacing of Tenascin-R," Nature Communications, Nature, vol. 12(1), pages 1-23, December.
    3. Claire Lacouture & Beatriz Chaves & Delphine Guipouy & Raïssa Houmadi & Valérie Duplan-Eche & Sophie Allart & Nicolas Destainville & Loïc Dupré, 2024. "LFA-1 nanoclusters integrate TCR stimulation strength to tune T-cell cytotoxic activity," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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