Septin

Septins are a conserved family of GTP-binding proteins found in nearly all eukaryotes except plants. They are classified as small GTPases and can self-assemble into hetero-oligomeric complexes that form filaments, rings, and other higher-order structures within cells. Septins act as cytoskeletal elements, particularly in cell division (cytokinesis), where they create scaffolds and diffusion barriers at specific cellular regions, thus regulating cell compartmentalization and polarity. They interact with cell membranes, actin filaments, and microtubules, and serve as attachment sites for other proteins, contributing to numerous cellular processes such as morphogenesis, membrane remodeling, and cilia organization. The dysregulation or mutation of septins has been implicated in cancer, neurodegenerative disease, and infertility, though therapeutic approaches directly targeting septins are at an early research stage[1][2][3][4][5][6]. No approved drugs currently target septins directly; their essential cellular roles present significant safety challenges for potential therapeutic intervention.

Other names

GTP-binding proteinP-Loop NTPaseSEPT1SEPT2SEPT3SEPT4SEPT5SEPT6SEPT7SEPT8SEPT9SEPT10SEPT11SEPT12SEPT14Cdc3Cdc10Cdc11Cdc12Shs1Spr3Spr28

No established mechanism for therapeutic agents; in principle, manipulation of septin filament assembly, GTPase activity, or protein-protein interactions may affect cell division and compartmentalization[1][2][4][5].