{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSEPTIN7 is a pivotal member of the septin family of GTP‐binding proteins that assemble into hetero‐oligomeric rod‐shaped complexes and nonpolar filaments, forming scaffolds that organize the cytoskeleton. High‐resolution structural and biochemical studies have revealed that SEPTIN7 occupies a unique, terminal position within hexameric or octameric building blocks, contributing essential elements of the conserved GTPase domain and terminal regions that mediate filament formation. In cultured cells and in vitro systems, SEPTIN7 co‐localizes with other septins along stress fibers and at sites of cell–cell contact, and its interaction network helps drive the assembly of higher order structures without obligatory involvement of predicted coiled‐coil domains. These findings underscore its fundamental architectural role in establishing diffusion barriers and platforms for protein recruitment."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its structural contributions, SEPTIN7 plays critical roles in mitosis, cell polarity and migration. It is essential for proper kinetochore recruitment of motor proteins during chromosome congression and for maintaining centrosome integrity and mitotic spindle organization, thereby ensuring accurate chromosome segregation. In polarizing epithelia and neurons, SEPTIN7‐containing filaments help guide microtubule plus‐end dynamics and reestablish cellular polarity after mitosis. In addition, SEPTIN7 participates in the formation and stabilization of primary cilia and podosomes and regulates endocytic events through its interaction with membrane receptors such as N‐cadherin. Disruption of SEPTIN7 levels or its regulatory modifications (including phosphorylation and SUMOylation) has been linked to aberrant actin dynamics and enhanced cancer cell migration, as well as to defects in endothelial barrier function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its functions in cytoskeletal organization and cell division, SEPTIN7 exerts diverse context‐dependent roles that impact cellular homeostasis and disease. It contributes to endosomal sorting mechanisms and the regulation of multivesicular body biogenesis, and it can modulate intracellular calcium influx by controlling store‐operated Ca²⁺ channels. Tissue‐specific expression studies indicate important roles during spermatogenesis and in thyroid and osteoblastic cells, where altered SEPTIN7 levels affect cell cycle progression and apoptosis. Moreover, its regulation by microRNAs and its sensitivity to posttranslational modifications such as PKA‐mediated phosphorylation highlight its capacity to integrate multiple signaling pathways and stress responses. Collectively, these multifaceted properties designate SEPTIN7 as a central regulatory hub whose perturbation is associated with tumorigenesis, neurodevelopmental disorders, and defective cell differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "29", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Minhajuddin Sirajuddin, Marian Farkasovsky, Florian Hauer, et al. 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