Two- or three-step assembly of banana-shaped proteins coupled with shape transformation of lipid membranes

Abstract

BAR superfamily proteins have a banana-shaped domain that causes the local bending of lipid membranes. We study as to how such a local anisotropic curvature induces effective interaction between proteins and changes the global shape of vesicles and membrane tubes using meshless membrane simulations. The proteins are modeled as banana-shaped rods strongly adhered to the membrane. Our study reveals that the rods assemble via two continuous directional phase separations unlike a conventional two-dimensional phase separation. As the rod curvature increases, in the membrane tube the rods assemble along the azimuthal direction and subsequently along the longitudinal direction accompanied by shape transformation of the tube. In the vesicle, in the addition to these two assembly processes, further increase in the rod curvature induces tubular scaffold formation.

6 pages, 8 figures

References in corpus (3)

• Membrane mediated aggregation of curvature inducing nematogens and membrane tubulation
• Anisotropic surface tension of buckled fluid membrane
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Cited by in corpus (6)

• Acceleration and suppression of banana-shaped-protein-induced tubulation by addition of small membrane inclusions of isotropic spontaneous curvatures
• Membrane shape deformation induced by curvature-inducing proteins consisting of chiral crescent binding and intrinsically disordered domains
• Binding of anisotropic curvature-inducing proteins onto membrane tubes
• Binding of Curvature-Inducing Proteins onto Biomembranes
• Membrane domain formation induced by binding/unbinding of curvature-inducing molecules onto both membrane surfaces
• Curvature-sensing and generation by membrane proteins: a review