Membrane-mediated protein interactions drive membrane protein organization

Yining Jiang, Batiste Thienpont, Vinay Sapuru, Richard K. Hite, Jeremy S. Dittman, James N. Sturgis and Simon Scheuring ()
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Yining Jiang: Weill Cornell Graduate School of Biomedical Sciences
Batiste Thienpont: Aix Marseille Université
Vinay Sapuru: Memorial Sloan Kettering Cancer Center
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

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-35202-8

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