SEPTIN1 is a filament-forming cytoskeletal GTPase that functions as a scaffolding protein in multiple cellular processes. Mechanistically, SEPTIN1 localizes to the midbody and spindle poles during mitosis, where it interacts with Aurora-B kinase that phosphorylates it at serine residues (248, 307, 315), regulating its role in cytokinesis and chromosome 16 1. At the Golgi apparatus, SEPTIN1 forms a scaffold dependent on GM130 and centrosomal proteins to promote microtubule nucleation and maintain Golgi ribbon integrity, with SEPTIN1 depletion causing Golgi fragmentation and impaired membrane trafficking 2. In epithelial cells, SEPTIN1 localizes to lamellipodia through actin-dependent mechanisms and forms complexes with SEPT4 and SEPT5 to regulate cell spreading and migration 3. Clinically, SEPTIN1 overexpression is associated with oral squamous-cell carcinoma progression, with 89% of tumors showing elevated expression compared to normal tissues, suggesting roles in cancer proliferation 4. SEPTIN1 was identified as a diagnostic biomarker for dilated cardiomyopathy, showing altered expression correlated with immune infiltration in cardiac tissue 5. Additionally, SEPTIN1 undergoes ubiquitination by Parkin E3 ligase, potentially influencing dopamine-related neurodegeneration and apoptosis pathways 6.