{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSENP3 is a SUMO-2/3–specific protease that functions as a sensitive redox sensor, integrating oxidative stress signals to modulate the SUMOylation status of numerous regulatory proteins. Under basal conditions, SENP3 is rapidly degraded, but modest increases in reactive oxygen species (ROS) not only stabilize SENP3 but also trigger its redistribution within the cell, thus influencing key nuclear events such as transcriptional activation (e.g., by deSUMOylating p300 to enhance hypoxia‐inducible factor‐1 activity) and inflammasome regulation via substrates like PML; these redox‐dependent regulatory modes have been documented in diverse stress settings including mild oxidative stress and ischaemia (see, for example."}, {"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": "\nBeyond its role as a sensor, SENP3 exerts critical control over mitochondrial dynamics and cell survival. By deSUMOylating the mitochondrial fission regulator Drp1, SENP3 facilitates Drp1 recruitment to the mitochondrial outer membrane via adaptors such as Mff, thereby promoting mitochondrial fission and, under stress conditions such as reperfusion after ischaemia, influencing cytochrome c release and apoptotic signalling. Moreover, SENP3‐dependent deSUMOylation has been implicated in mitophagy through substrates like FIS1, highlighting its role in quality control of mitochondrial turnover."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}, {"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nucleolus, SENP3 is intimately involved in ribosome biogenesis. It partners with key nucleolar proteins such as nucleophosmin (NPM1) and B23, participating in dynamic SUMOylation–deSUMOylation cycles that are essential for the proper processing of ribosomal RNA and maturation of the 60S ribosomal subunit. These actions underscore its pivotal role in sustaining protein synthesis and cell proliferation, as evidenced by its association with factors like PELP1 and regulatory components of the SET1/MLL histone methyltransferase complexes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "12"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSENP3 also plays a central role in maintaining genome integrity and proper cell cycle progression. During mitosis, it regulates the SUMOylation status of several chromosome-associated proteins. For instance, its deSUMOylation of substrates such as Borealin, Topoisomerase IIα, Aurora A, and MRE11 facilitates correct mitotic events including spindle assembly, chromosome segregation, and DNA end resection. Moreover, precise phosphorylation of SENP3 during mitosis modulates its own activity, ensuring genomic stability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "17"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThrough its deSUMOylating activity, SENP3 modulates multiple transcriptional regulators and signaling pathways that are central to cell fate decisions in both normal physiology and disease. It affects transcription by altering the SUMOylation status of key co-activators and transcription factors such as p300, FOXC2, STAT3, Sp1, and components of the 5FMC complex, thereby regulating processes ranging from hypoxia response and epithelial–mesenchymal transition (EMT) to the p53–MDM2 feedback loop and even the ubiquitin-dependent degradation of substrates like PARIS. These diverse effects position SENP3 as an important mediator of transcription programs that influence cell proliferation, differentiation, and survival."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "23"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of SENP3 has been implicated in the pathology of various human diseases, particularly cancers and metabolic disorders. Overexpression or aberrant regulation of SENP3 is observed in multiple tumor types—including oral squamous cell carcinoma, osteosarcoma, pancreatic ductal adenocarcinoma, mantle cell lymphoma, esophageal carcinoma, and triple‐negative breast cancer—where it modulates tumor cell proliferation, migration, invasion, and EMT (sometimes via targets such as E-cadherin or YAP1). In addition, SENP3 has been linked to metabolic conditions such as non‐alcoholic fatty liver disease and bone loss, and it influences host–pathogen interactions in hepatitis B infection as well as inflammatory responses in chronic rhinosinusitis. These findings suggest that SENP3 is a key regulatory hub whose context-dependent modulation of SUMOylation status contributes not only to stress responses and genome maintenance but also to the progression of cancers and various metabolic and inflammatory disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "34"}]}, {"type": "t", "text": " \n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional studies have unveiled further nuances in SENP3 regulation. For instance, its interactions within complexes (such as the 5FMC, whose assembly depends on arginine methylation) connect SUMO deconjugation to broader chromatin and transcription regulatory mechanisms"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "35"}]}, {"type": "t", "text": "remains part of this landscape), while recent work has also implicated SENP3 in the control of DNA repair processes through modulation of end resection and in shaping the cellular ubiquitination landscape by impairing SUMO-targeted ubiquitin ligases. Though investigations continue—for example, into the genetic underpinnings of its expression patterns"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "36"}]}, {"type": "t", "text": "or its emerging roles in ferroptosis"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "37"}]}, {"type": "t", "text": "—SENP3 is increasingly recognized as a multifaceted enzyme bridging post-translational modifications with diverse cellular outcomes.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Chao Huang, Yan Han, Yumei Wang, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/emboj.2010.245"}], "href": "https://doi.org/10.1038/emboj.2010.245"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20924358"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20924358"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Chun Guo, Keri L Hildick, Jia Luo, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "SENP3-mediated de-conjugation of SUMO2/3 from promyelocytic leukemia is correlated with accelerated cell proliferation under mild oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.071431"}], "href": "https://doi.org/10.1074/jbc.M109.071431"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20181954"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20181954"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Chun Guo, Kevin A Wilkinson, Ashley J Evans, et al. "}, {"type": "b", "children": [{"type": "t", "text": "SENP3-mediated deSUMOylation of Drp1 facilitates interaction with Mff to promote cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep43811"}], "href": "https://doi.org/10.1038/srep43811"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28262828"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28262828"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Lingchen Gao, Yichao Zhao, Jie He, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The desumoylating enzyme sentrin-specific protease 3 contributes to myocardial ischemia reperfusion injury."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Genet Genomics (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jgg.2017.12.002"}], "href": "https://doi.org/10.1016/j.jgg.2017.12.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29576508"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29576508"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Kevin A Wilkinson, Chun Guo "}, {"type": "b", "children": [{"type": "t", "text": "Iron chelation promotes mitophagy through SENP3-mediated deSUMOylation of FIS1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/15548627.2022.2046898"}], "href": "https://doi.org/10.1080/15548627.2022.2046898"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35275026"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35275026"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Markus Haindl, Thomas Harasim, Dirk Eick, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/embor.2008.3"}], "href": "https://doi.org/10.1038/embor.2008.3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18259216"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18259216"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Chawon Yun, Yonggang Wang, Debaditya Mukhopadhyay, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200807185"}], "href": "https://doi.org/10.1083/jcb.200807185"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19015314"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19015314"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Nithya Raman, Arnab Nayak, Stefan Muller "}, {"type": "b", "children": [{"type": "t", "text": "mTOR signaling regulates nucleolar targeting of the SUMO-specific isopeptidase SENP3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00801-14"}], "href": "https://doi.org/10.1128/MCB.00801-14"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25288641"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25288641"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Jayonta Bhattacharjee, Sruthi Alahari, Julien Sallais, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dynamic regulation of HIF1Α stability by SUMO2/3 and SENP3 in the human placenta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Placenta (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.placenta.2016.02.002"}], "href": "https://doi.org/10.1016/j.placenta.2016.02.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27016777"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27016777"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Nithya Raman, Elisabeth Weir, Stefan Müller "}, {"type": "b", "children": [{"type": "t", "text": "The AAA ATPase MDN1 Acts as a SUMO-Targeted Regulator in Mammalian Pre-ribosome Remodeling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2016.09.039"}], "href": "https://doi.org/10.1016/j.molcel.2016.09.039"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27814492"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27814492"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Ulf R Klein, Markus Haindl, Erich A Nigg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e08-05-0511"}], "href": "https://doi.org/10.1091/mbc.e08-05-0511"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18946085"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18946085"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Bo Wei, Chao Huang, Bin Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitotic Phosphorylation of SENP3 Regulates DeSUMOylation of Chromosome-Associated Proteins and Chromosome Stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-17-2288"}], "href": "https://doi.org/10.1158/0008-5472.CAN-17-2288"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29438989"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29438989"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Tao Zhang, Han Yang, Zenan Zhou, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Crosstalk between SUMOylation and ubiquitylation controls DNA end resection by maintaining MRE11 homeostasis on chromatin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-022-32920-x"}], "href": "https://doi.org/10.1038/s41467-022-32920-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36050397"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36050397"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Bin Yu, Qiaoyu Lin, Chao Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "SUMO proteases SENP3 and SENP5 spatiotemporally regulate the kinase activity of Aurora A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.249771"}], "href": "https://doi.org/10.1242/jcs.249771"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34313310"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34313310"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Zhuo Li, Jian Liu, Huifeng Fu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "SENP3 affects the expression of PYCR1 to promote bladder cancer proliferation and EMT transformation by deSUMOylation of STAT3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Aging (Albany NY) (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/aging.204333"}], "href": "https://doi.org/10.18632/aging.204333"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36227136"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36227136"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Tamotsu Nishida, Yoshiji Yamada "}, {"type": "b", "children": [{"type": "t", "text": "The nucleolar SUMO-specific protease SMT3IP1/SENP3 attenuates Mdm2-mediated p53 ubiquitination and degradation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2011.02.034"}], "href": "https://doi.org/10.1016/j.bbrc.2011.02.034"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21316347"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21316347"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Pavlos Fanis, Nynke Gillemans, Ali Aghajanirefah, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Five friends of methylated chromatin target of protein-arginine-methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation to desumoylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M112.017194"}], "href": "https://doi.org/10.1074/mcp.M112.017194"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22872859"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22872859"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Arnab Nayak, Sandra Viale-Bouroncle, Christian Morsczeck, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The SUMO-specific isopeptidase SENP3 regulates MLL1/MLL2 methyltransferase complexes and controls osteogenic differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2014.05.011"}], "href": "https://doi.org/10.1016/j.molcel.2014.05.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24930734"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24930734"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Yan-hua Ren, Ke-jia Liu, Ming Wang, et al. 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