Membrane shape deformation induced by curvature-inducing proteins consisting of chiral crescent binding and intrinsically disordered domains

TL;DR

This study uses meshless membrane simulations to explore how intrinsically disordered domains in curvature-inducing proteins influence membrane deformation, revealing diverse shapes and assembly behaviors based on chain length and curvature.

Contribution

It introduces a novel simulation model combining protein and membrane interactions, highlighting the role of disordered chains in membrane shape regulation.

Findings

Longer disordered chains reduce protein cluster size.

Disordered chains induce spindle-shaped vesicles and tubules.

Protein curvature and chain length determine membrane morphology.

Abstract

Curvature-inducing proteins containing a Bin/Amphiphysin/Rvs domain often have intrinsically disordered domains. Recent experiments have shown that these disordered chains enhance curvature sensing and generation. Here, we report on the modification of protein-membrane interactions by disordered chains using meshless membrane simulations. The protein and bound membrane are modeled together as a chiral crescent protein rod with two excluded-volume chains. As the chain length increases, the repulsion between them reduces the cluster size of the proteins. It induces spindle-shaped vesicles and a transition between arc-shaped and circular protein assemblies in a disk-shaped vesicle. For flat membranes, an intermediate chain length induces many tubules owing to the repulsion between the protein assemblies, whereas longer chains promote perpendicular elongation of tubules. Moreover, protein rods with zero rod curvature and sufficiently long chains stabilize the spherical buds. For proteins with a negative rod curvature, an intermediate chain length induces a rugged membrane with branched protein assemblies, whereas longer chains induce the formation of tubules with periodic concave-ring structures.