A balance of attractive and repulsive forces controls the direction of membrane bending by intrinsically disordered proteins

The ability of proteins to generate membrane curvature is essential to many cellular functions. Previously characterized membrane bending mechanisms rely on protein domains with specific structural features like amphipathic helices and curved scaffolds. However, more recent work has shown that intrinsically disordered proteins (IDPs) can be potent drivers of membrane bending. Specifically, IDPs that repel on another can drive formation of protein-coated tubules through steric pressure, when crowded on the membrane.