Directional interactions and cooperativity between mechanosensitive membrane proteins
arXiv:1209.3083 · doi:10.1209/0295-5075/101/68002
Abstract
While modern structural biology has provided us with a rich and diverse picture of membrane proteins, the biological function of membrane proteins is often influenced by the mechanical properties of the surrounding lipid bilayer. Here we explore the relation between the shape of membrane proteins and the cooperative function of membrane proteins induced by membrane-mediated elastic interactions. For the experimental model system of mechanosensitive ion channels we find that the sign and strength of elastic interactions depend on the protein shape, yielding distinct cooperative gating curves for distinct protein orientations. Our approach predicts how directional elastic interactions affect the molecular structure, organization, and biological function of proteins in crowded membranes.
References in corpus (1)
Cited by in corpus (15)
- Perspective: Geometrically-Frustrated Assemblies
- Bilayer-thickness-mediated interactions between integral membrane proteins
- Attractive asymmetric inclusions in elastic membranes under tension: cluster phases and membrane invaginations
- Architecture and Function of Mechanosensitive Membrane Protein Lattices
- Protein recruitment through indirect mechanochemical interactions
- Composition variation and underdamped mechanics near membrane proteins and coats
- Role of the membrane for mechanosensing by tethered channels
- Symmetry and size of membrane protein polyhedral nanoparticles
- Signatures of protein structure in the cooperative gating of mechanosensitive ion channels
- Signatures of Mechanosensitive Gating
- Membrane-mediated interactions
- Controlling the shape of membrane protein polyhedra
- Dependence of protein-induced lipid bilayer deformations on protein shape
- Thermodynamic competition between membrane protein oligomeric states
- Curvature Instability of Membranes near Rigid Inclusions