Membrane tension controls the assembly of curvature-generating proteins

Mijo Simunovic and Gregory A. Voth ()
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Mijo Simunovic: Institute for Biophysical Dynamics, James Franck Institute and Computation Institute, The University of Chicago
Gregory A. Voth: Institute for Biophysical Dynamics, James Franck Institute and Computation Institute, The University of Chicago

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Proteins containing a Bin/Amphiphysin/Rvs (BAR) domain regulate membrane curvature in the cell. Recent simulations have revealed that BAR proteins assemble into linear aggregates, strongly affecting membrane curvature and its in-plane stress profile. Here, we explore the opposite question: do mechanical properties of the membrane impact protein association? By using coarse-grained molecular dynamics simulations, we show that increased surface tension significantly impacts the dynamics of protein assembly. While tensionless membranes promote a rapid formation of long-living linear aggregates of N-BAR proteins, increase in tension alters the geometry of protein association. At high tension, protein interactions are strongly inhibited. Increasing surface density of proteins leads to a wider range of protein association geometries, promoting the formation of meshes, which can be broken apart with membrane tension. Our work indicates that surface tension may play a key role in recruiting proteins to membrane-remodelling sites in the cell.

Date: 2015
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DOI: 10.1038/ncomms8219

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