Septin-2 is a filament-forming cytoskeletal GTPase. It forms a filamentous structure with other septins such as SEPT6, SEPT7, and SEPT12. This structure is crucial for the integrity and motility of the sperm tail during postmeiotic differentiation . The recombinant form of Septin-2 is typically expressed in Escherichia coli and is purified to a high degree of purity (>90%) using conventional chromatography techniques .
Cytokinesis: Septin-2 plays a critical role in cytokinesis, the process by which a cell divides its cytoplasm to produce two daughter cells. It forms a scaffold at the midplane of the mitotic spindle, which is essential for maintaining the localization of CENPE at kinetochores and ensuring proper chromosome congression .
Actin Cytoskeleton Organization: Septin-2 is required for the normal organization of the actin cytoskeleton. It helps maintain polyglutamylated microtubules, facilitating efficient vesicle transport and impeding MAP4 binding to tubulin .
Ciliogenesis: In cilia, Septin-2 is necessary for the integrity of the diffusion barrier at the base of the primary cilium. This barrier prevents the diffusion of transmembrane proteins between the cilia and plasma membranes .
Cell Movement: Septin-2 also plays a role in collective cell movements, which are essential for various developmental processes and wound healing .