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Membrane-mediated protein interactions drive membrane protein organization
Yining Jiang1,2, Batiste Thienpont3, Vinay Sapuru4,5
1Biochemistry & Structural Biology, Cell & Developmental Biology, and Molecular Biology (BCMB) Program, Weill Cornell Graduate School of Biomedical Sciences, 1300 York Avenue, New York, NY, 10065, USA.
Nature Communications
|November 30, 2022
Summary
Membrane proteins self-organize within lipid bilayers, driven by hydrophobic mismatch and thermal motion. This study reveals how basic physical properties govern the emergence of membrane organization without active processes.
Area of Science:
- Biophysics
- Cell Biology
- Materials Science
Background:
- Plasma membranes feature organized lipid-protein domains and supercomplexes.
- The mechanisms establishing membrane organization are not fully understood.
- Thermal fluctuations and protein interactions are key factors.
Purpose of the Study:
- Investigate model membrane protein oligomerization and assembly.
- Explore the role of lipid environments in membrane organization.
- Understand emergent membrane organization from physical principles.
Main Methods:
- High-speed atomic force microscopy (HS-AFM).
- Kinetic and membrane elastic theory.
- Controlled lipid environments for model membrane proteins.
Main Results:
- Hydrophobic mismatch significantly modulates protein oligomerization and assembly energetics.
- Hydrophobic mismatch influences two-dimensional (2D) organization within the membrane.
- Demonstrated emergence of membrane organization from Brownian motion and intrinsic physical properties.
Conclusions:
- Membrane organization can arise intrinsically from physical interactions.
- Hydrophobic mismatch is a critical determinant of protein assembly and spatial organization.
- Brownian diffusion and membrane properties explain emergent membrane organization.
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