title: Membrane tension controls the assembly of curvature-generating proteins.
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.
authors.affiliation: Department of Chemistry, Institute for Biophysical Dynamics, James Franck Institute and Computation Institute, The University of Chicago, 5735 S Ellis Avenue, Chicago, Illinois 60637, USA.
authors.forename: Mijo
authors.initials: M
authors.lastname: Simunovic
authors.affiliation: Department of Chemistry, Institute for Biophysical Dynamics, James Franck Institute and Computation Institute, The University of Chicago, 5735 S Ellis Avenue, Chicago, Illinois 60637, USA.
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Voth
mesh_terms: D002462:Cell Membrane / Q000502:physiology*; D008954:Models, Biological; D056004:Molecular Dynamics Simulation; D055503:Protein Multimerization; D011506:Proteins / Q000378:metabolism*; D013500:Surface Tension
chemical_list: D011506:Proteins