Abstract
This review examines the relationships between membrane chemistry, curvature-sensing proteins, and cellular morphogenesis. Curvature-sensing proteins are often orders of magnitude smaller than the membrane curvatures they localize to. How are nanometer-scale proteins used to sense micrometer-scale membrane features? Here, we trace the journey of curvature-sensing proteins as they engage with lipid membranes through a combination of electrostatic and hydrophobic interactions. We discuss how curvature sensing hinges on membrane features like lipid charge, packing, and the directionality of membrane curvature. Once bound to the membrane, many curvature sensors undergo self-assembly (i.e., they oligomerize or form higher-order assemblies that are key for initiating and regulating cell shape transformations). Central to these discussions are the micrometer-scale curvature-sensing proteins' septins. By discussing recent literature surrounding septin membrane association, assembly, and their many functions in morphogenesis with support from other well-studied curvature sensors, we aim to synthesize possible mechanisms underlining cell shape sensing.