Stability of a biomembrane tube covered with proteins

Abstract

Membrane tubes are essential structural features in cells that help facilitate biomaterial transport and inter- and intracellular signalling. The shape of these tubes can be regulated by the proteins that surround and adhere to them. We study here the stability of a biomembrane tube coated with proteins by combining linear stability analysis and numerical solutions of a Helfrich-like membrane model. Our analysis demonstrates that both long and short wavelength perturbations can destabilise the tubes. Numerical simulations confirm the derived linear stability criteria and also yield the nonlinearly-perturbed vesicle shapes. Our analysis highlights the interplay between the membrane shape and the protein density, where the shape instability concurs with a redistribution of proteins into a banded pattern.

Formation of membrane invaginations by curvature-inducing peripheral proteins: free energy profiles, kinetics, and membrane-mediated effects

“…Tourdot et al used a continuum membrane model with curvature fields and monitored the change in excess chemical potential of membrane-bending proteins to mark the tubulation threshold [18]. Mathijs et al considered a Ginzburg-Landau-type free energy for the protein coat and discussed the stability of the cylindrical tubes covered with proteins [19]. Mahapatra and Rangamani developed a theoretical model to estimate the free energy of membrane tubulation due to bound BAR-domain proteins with anisotropic curvature, and showed the snapthrough characteristics in the dome-to-cylinder transitions [20] Here we offer a fresh take on this problem, using a mesoscopic dynamical membrane model [21].…”

“…In another approach, Tourdot et al employed a continuum membrane model alongside curvature fields, tracking changes in the excess chemical potential of membrane-bending proteins to pinpoint the tubulation threshold [26]. Mathijs et al adopted a Ginzburg-Landau-style free energy for the protein coat, examining the stability of cylindrical tubes adorned with proteins [27]. Further-more, Mahapatra and Rangamani constructed a theoretical framework estimating the free energy of membrane tubulation resulting from bound BAR-domain proteins exhibiting anisotropic curvature.…”