Structural symmetry and membrane curvature sensing

TL;DR

This paper investigates how the structural symmetry of membrane proteins influences their ability to sense and induce membrane curvature, revealing that asymmetry enhances directional sensing while symmetry suppresses it.

Contribution

It provides a theoretical framework linking protein symmetry to membrane curvature sensing, highlighting the importance of asymmetry for directional sensing capabilities.

Findings

Asymmetric proteins can sense direction-dependent membrane curvature.

Symmetric proteins, especially with higher symmetry, suppress directional sensing.

Dimeric proteins exhibit the strongest anisotropic curvature sensing.

Abstract

Symmetry is closely intertwined with the function, genetics, and chemical properties of multiprotein complexes. Here, we explore the relation between structural symmetry and the ability of membrane proteins to sense and induce membrane curvature, which is a key factor for modulating the shape and organization of cell membranes. Using coarse-grained simulations and elasticity theory, we show that the potential for direction-dependent membrane curvature sensing is limited to asymmetric proteins, dimers, and tetramers, and argue that one should expect this anisotropy to be strongest for dimers. Odd and higher-order symmetries strongly suppress directional curvature sensing. This classification gives a new perspective on the structure-function relation for membrane proteins, and simplifies the task of translating between molecular sensing mechanisms and their large-scale cellular consequences.