{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSENP2 is an evolutionarily conserved SUMO‐specific protease that plays dual roles in SUMO maturation and de‐conjugation. It is dynamically targeted to key subcellular locales including the nuclear pore complex and kinetochore. In human cells, SENP2 associates via sequences near its N terminus with nucleoporins such as Nup153 and components of the Nup107–160 subcomplex, and its nucleocytoplasmic shuttling is orchestrated by a bipartite nuclear localization signal and a CRM1‐dependent nuclear export signal. Structural studies further reveal that its catalytic domain is optimized for recognizing specific SUMO conjugates."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its subcellular positioning, SENP2 exerts critical control over multiple signaling pathways. It contributes to proper trophoblast development by regulating the SUMOylation status of Mdm2 and, consequently, p53 degradation. SENP2 also modulates NF‑κB activation by deSUMOylating NEMO, a key mediator in the DNA damage response, and promotes efficient double‐strand break repair by restraining excessive SUMOylation of MDC1 to facilitate nonhomologous end joining. In addition, SENP2 influences TGF‑β signaling—through deSUMOylation of pathway components—to affect epithelial–mesenchymal transitions and cell migration, a process further echoed by its emerging role in mitigating chemoresistance in hematological malignancies."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSENP2 is also a central regulator of metabolic and developmental programs. In cardiovascular development, a balanced SENP2 activity is essential for normal cardiogenesis. In skeletal muscle, deSUMOylation of peroxisome proliferator‐activated receptors by SENP2 enhances fatty acid oxidation, thereby alleviating high‐fat diet–induced metabolic disorders. Its ability to deSUMOylate transcription factors such as MEF2A under activity‐dependent conditions illuminates a mechanism whereby SENP2 fine‐tunes gene expression during development. In addition, SENP2 modulates glucose metabolism by repressing glycolysis via attenuation of AKT phosphorylation, and in pancreatic β cells, SENP2 influences mitochondrial dynamics and insulin secretion through regulation of DRP1 phosphorylation and SDHA SUMOylation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn oncology, SENP2 has emerged as a potent tumor suppressor through its capacity to modulate oncogenic signaling pathways. Its deSUMOylation activity contributes to the destabilization of β‑catenin and the suppression of estrogen receptor–driven transcription in breast cancer, while also engaging with proteins such as WWOX to regulate β‑catenin stability in hepatocellular carcinoma. Moreover, alterations in SENP2—whether by differential expression, genetic polymorphism, or aberrant post‑translational regulation—have been linked to invasive phenotypes in bladder cancer, chronic lymphocytic leukemia, and epithelial malignancies where it governs checkpoints that intersect mitosis and differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jun Hang, Mary Dasso "}, {"type": "b", "children": [{"type": "t", "text": "Association of the human SUMO-1 protease SENP2 with the nuclear pore."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M201799200"}], "href": "https://doi.org/10.1074/jbc.M201799200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11896061"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11896061"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yoko Itahana, Edward T H Yeh, Yanping Zhang "}, {"type": "b", "children": [{"type": "t", "text": "Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01830-05"}], "href": "https://doi.org/10.1128/MCB.01830-05"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16738331"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16738331"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "David Reverter, Christopher D Lima "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Struct Mol Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nsmb1168"}], "href": "https://doi.org/10.1038/nsmb1168"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17099700"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17099700"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Jacqueline Goeres, Pak-Kei Chan, Debaditya Mukhopadhyay, et al. 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