{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSEPTIN4, predominantly expressed as the ARTS isoform, plays a pivotal role in promoting mitochondrial apoptosis and acting as a tumor suppressor. ARTS antagonizes inhibitor‐of‐apoptosis proteins such as XIAP and Bcl‑2, thereby facilitating caspase activation in response to diverse pro‐apoptotic stimuli. In several cancer models—including acute lymphoblastic leukemia and hepatocellular carcinoma—the loss or down‑regulation of SEPTIN4/ARTS correlates with resistance to apoptosis. Notably, SEPTIN4 is transcriptionally regulated by p53 and is subject to ubiquitin‑mediated proteolysis via factors like AREL1, highlighting its critical function in maintaining cellular homeostasis through selective protein degradation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn neural tissue, SEPTIN4 functions as a scaffold that interacts with key presynaptic proteins including alpha‑synuclein. This association helps to protect against aberrant self‑aggregation and pathological phosphorylation that are hallmarks of Lewy body formation in Parkinson’s disease. Moreover, structural investigations reveal that the central GTPase domain of SEPTIN4 can form partially unfolded, amyloid‑like aggregates, suggesting that misfolded forms of SEPTIN4 might contribute to neurodegenerative processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in apoptosis and neural homeostasis, SEPTIN4 is essential for a variety of cellular processes linked to cytoskeletal organization and specialized structure formation. In spermatozoa, SEPTIN4 is a key component of the annulus—a ring‐like structure vital for maintaining midpiece–principal piece integrity—and loss‑of‑function mutations are associated with asthenoteratozoospermia. SEPTIN4 also forms heteromeric complexes with other septins (e.g., SEPT5 and SEPT8) that regulate platelet secretion, while its interactions with factors such as PARP1 implicate it in endothelial injury and vascular remodeling. In hepatic stellate cells, altered SEPTIN4 expression influences apoptosis and fibrosis, and its dysregulation, along with associations to Notch signaling, serves as a potential diagnostic marker in various cancers (including bladder and colorectal malignancies), as well as in neuropsychiatric and bone metabolism disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "32"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yossi Gottfried, Asaf Rotem, Rona Lotan, et al. 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