Membrane protein clustering from tension and multibody interactions

TL;DR

This paper demonstrates how membrane tension and multibody interactions influence protein clustering, revealing mechanisms for phase separation and cluster dissolution relevant to biological membranes.

Contribution

It introduces a point-curvature model that captures multibody interactions and elucidates how tension affects protein clustering and phase behavior.

Findings

Membrane tension enhances many-body repulsion between identical curved proteins.

Oppositely curved proteins tend to form antiferromagnetic square lattice structures.

Increased tension can dissolve protein clusters stabilized by short-range forces.

Abstract

The point-curvature model for membrane protein inclusions is shown to capture multibody interactions very well. Using this model, we find that the interplay between membrane tension and multibody interactions results in a collective attraction of oppositely curved inclusions tending to form antiferromagnetic structures with a square lattice. This attraction can produce a phase separation between curved and non-curved proteins, resulting in the clustering of curved proteins. We also show that the many-body repulsion between identical curved proteins is enhanced by membrane tension. This can lead to the dissolution of clusters stabilized by short-range forces when the tension is increased. These new phenomena are biologically relevant and could be investigated experimentally