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Membrane-mediated protein interactions drive membrane protein organization

Author

Listed:
  • Yining Jiang

    (Weill Cornell Graduate School of Biomedical Sciences
    Weill Cornell Medicine, Department of Anesthesiology)

  • Batiste Thienpont

    (Aix Marseille Université)

  • Vinay Sapuru

    (Memorial Sloan Kettering Cancer Center
    Weill Cornell Graduate School of Biomedical Sciences)

  • Richard K. Hite

    (Memorial Sloan Kettering Cancer Center)

  • Jeremy S. Dittman

    (Weill Cornell Medicine, Department of Biochemistry)

  • James N. Sturgis

    (Aix Marseille Université)

  • Simon Scheuring

    (Weill Cornell Medicine, Department of Anesthesiology
    Weill Cornell Medicine, Department of Physiology and Biophysics
    Cornell University)

Abstract

The plasma membrane’s main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents.

Suggested Citation

  • Yining Jiang & Batiste Thienpont & Vinay Sapuru & Richard K. Hite & Jeremy S. Dittman & James N. Sturgis & Simon Scheuring, 2022. "Membrane-mediated protein interactions drive membrane protein organization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-35202-8
    DOI: 10.1038/s41467-022-35202-8
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    References listed on IDEAS

    as
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    1. Yat Ho Chan & Koralege C. Pathmasiri & Dominick Pierre-Jacques & Maddison C. Hibbard & Nannan Tao & Joshua L. Fischer & Ethan Yang & Stephanie M. Cologna & Ruixuan Gao, 2024. "Gel-assisted mass spectrometry imaging enables sub-micrometer spatial lipidomics," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Emma C. Couves & Scott Gardner & Tomas B. Voisin & Jasmine K. Bickel & Phillip J. Stansfeld & Edward W. Tate & Doryen Bubeck, 2023. "Structural basis for membrane attack complex inhibition by CD59," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    3. 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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