Issue 17, 2022

Binding of anisotropic curvature-inducing proteins onto membrane tubes

Abstract

Bin/Amphiphysin/Rvs superfamily proteins and other curvature-inducing proteins have anisotropic shapes and anisotropically bend biomembranes. Here, we report how the anisotropic proteins bind the membrane tube and are orientationally ordered using mean-field theory including an orientation-dependent excluded volume. The proteins exhibit a second-order or first-order nematic transition with increasing protein density depending on the radius of the membrane tube. The tube curvatures for the maximum protein binding and orientational order are different and varied by the protein density and rigidity. As the external force along the tube axis increases, a first-order transition from a large tube radius with low protein density to a small radius with high density occurs once, and subsequently, the protein orientation tilts to the tube-axis direction. When an isotropic bending energy is used for the proteins with an elliptic shape, the force-dependence curves become symmetric and the first-order transition occurs twice. This theory quantitatively reproduces the results of meshless membrane simulation for short proteins, whereas deviations are seen for long proteins owing to the formation of protein clusters.

Graphical abstract: Binding of anisotropic curvature-inducing proteins onto membrane tubes

Supplementary files

Article information

Article type
Paper
Submitted
28 Feb 2022
Accepted
04 Apr 2022
First published
05 Apr 2022

Soft Matter, 2022,18, 3384-3394

Author version available

Binding of anisotropic curvature-inducing proteins onto membrane tubes

H. Noguchi, C. Tozzi and M. Arroyo, Soft Matter, 2022, 18, 3384 DOI: 10.1039/D2SM00274D

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