BN forum SaFyre Reese

Cells require diffusion barriers and compartmentalization from scaffolding proteins, such as septins. As the fourth component of the cytoskeleton, septins play an important role in maintaining cell morphology and may have implications in processes like cancer cell migration. In vitro, septins have been shown to directly bind to membranes and are capable of anchoring actin. We aim to bridge the gap between the nanoscale spatial arrangement of septin networks and their impact on cellular shape and behavior, by studying septin organization in model systems. Using quartz crystal microbalance (QCM-D), we measured septin binding kinetics on supported lipid bilayers. Atomic force microscopy (AFM) and transmission electron microscopy (TEM) provided insights into the end state network architectures formed on supported bilayers and lipid monolayers, respectively. Depending on lipid composition and septin isoform, septins formed either bundled or cross-hatched networks. Understanding the architecture and organization of septin networks on membranes offers insights into their potential roles in cellular mechanical properties and may provide a foundation for further exploration of their functions in cell mechanics and morphology.

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