{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSENP1 is a SUMO‐specific protease that plays a central role in both the maturation of SUMO proteins and the removal of SUMO modifications from a myriad of substrates. Detailed biochemical and structural studies have shown that SENP1 preferentially processes SUMO‑1 over closely related paralogues because of unique electrostatic interactions at its active site, and structural snapshots of the enzyme–substrate complex have clarified the orientation of the scissile bond required for catalysis. In addition, SENP1 activity is modulated by oxidative cues; under oxidative stress, reversible disulfide bond formation at its active site helps preserve protease function, thereby acting as a redox sensor and protecting the enzyme from irreversible inactivation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBy selectively reversing SUMOylation on key transcription factors and their cofactors, SENP1 orchestrates several oncogenic and transcription‐dependent signaling pathways. In prostate and other cancers, SENP1 enhances androgen receptor–mediated transcription—not only by deSUMOylating the receptor itself but also by diminishing the repressive influences of factors like histone deacetylase 1—thereby stimulating the expression of oncogenic targets such as cyclin D1. In addition, SENP1 stabilizes oncoproteins including c‑Myc and Pin1 via deSUMOylation, and aberrations such as gene fusions involving SENP1 have been linked to tumor progression. A network of microRNAs (for example, miR‑138, miR‑145, and miR‑133a‑3p) further modulates SENP1 expression, underscoring its importance as a prognostic marker and therapeutic target in cancers such as prostate, colon, and lung carcinoma."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its cancer‐related functions, SENP1 contributes broadly to tissue homeostasis and metabolic regulation. In pancreatic β cells, SENP1‐mediated deSUMOylation amplifies insulin exocytosis, while in endothelial cells it facilitates hypoxia‐induced expression of vascular endothelial growth factor by stabilizing hypoxia‑inducible factor signaling, thereby promoting angiogenesis. SENP1 also plays cardioprotective roles by modulating mitochondrial biogenesis through the deSUMOylation of transcriptional coactivators, and it influences epithelial–mesenchymal transition in hepatocellular carcinoma as well as glycolytic reprogramming in clear cell renal cell carcinoma. Moreover, in response to proinflammatory stimuli, SENP1 directs the deSUMOylation of factors such as HIPK1, thereby modulating apoptotic signaling cascades. Its involvement in regulating OCT4 stability further implicates SENP1 in controlling cell fate decisions during aberrant erythropoiesis, as observed in high‐altitude polycythemia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, SENP1 helps maintain nuclear integrity and genome stability by localizing to the nuclear periphery, where it partners with nucleoporins to regulate the sumoylation status of DNA damage response factors such as 53BP1. 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