{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSET is emerging as a multifunctional oncoprotein that critically influences cancer cell signaling through its potent inhibition of protein phosphatase 2A (PP2A). In BCR/ABL‐transformed cells and other hematologic malignancies, induced SET expression suppresses PP2A‐mediated dephosphorylation of key oncogenic regulators such as c‐Myc, thereby promoting cell proliferation and survival. Overexpression of SET has been implicated in breast cancer, acute myeloid leukemia, and head and neck carcinomas, while strategies antagonizing SET (for example, by SET‐inhibitory peptides) have been shown to restore PP2A activity and counteract tumorigenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its role in oncogenic signal amplification, SET functions as a key regulator of transcription and chromatin structure. The molecule can bind unacetylated lysine‐rich tails of histones and of p53—through its acidic domains acting as a “reader” for hypoacetylated sequences—thereby repressing p53‐dependent transcription. Moreover, SET is a component of the inhibitor of histone acetyltransferases (INHAT) complex and exhibits histone chaperone activity; it even forms oncogenic fusion proteins (SET–NUP214) that aberrantly activate HOXA gene clusters in T‐cell acute lymphoblastic leukemia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSET also plays a pivotal role in cell cycle regulation and kinase signaling. It interacts directly with the cell cycle inhibitor p21 and contributes to the inhibition of cyclin B–CDK1 activity, thereby affecting the G₂/M transition. In parallel, SET can stimulate the activity of Aurora-A kinase by binding via distinct domains, and it competes with regulators such as TSPX for cyclin B1 association, collectively ensuring proper cell division and, when dysregulated, contributing to oncogenic proliferation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "18"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond control of proliferation, SET modulates cellular motility and genomic stability. It is recruited to the plasma membrane by active Rac1 to facilitate cell migration, and as part of the SET complex it participates in caspase‐independent cell death pathways—where granzyme A cleaves SET, triggering localized single‐strand DNA damage. In parallel, under conditions of acidosis, SET becomes a substrate of proteases such as asparagine endopeptidase, an event linked to neuronal injury. Furthermore, SET’s interaction with cytochrome c can lock its histone chaperone domains, thereby modulating chromatin accessibility and influencing the DNA damage response."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "23"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nervous system, mislocalization and post‐translational modifications of SET have been linked to neurodegenerative pathology. Phosphorylation of SET at critical serine residues leads to its cytoplasmic accumulation in Alzheimer’s disease neurons, where it contributes to PP2A inhibition and consequent tau hyperphosphorylation, fostering neurofibrillary tangle formation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n\n"}]}, {"type": "t", "text": "\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, SET’s regulatory capabilities extend to endocrine functions; by inhibiting PP2A activity, SET modulates the serine phosphorylation status of enzymes such as cytochrome P450c17, thereby enhancing 17,20 lyase activity and influencing androgen biosynthesis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Paolo Neviani, Ramasamy Santhanam, Rossana Trotta, et al. 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