{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMultifunctional ZNF35 (commonly known in these studies as nardilysin or NRDc) is emerging as a pivotal metalloendopeptidase modulating proteolytic processing and ectodomain shedding. It directly cleaves peptide precursors at both di‐ and mono‐basic sites, thereby generating bioactive fragments such as miniglucagon and modulating the α‐secretase cleavage of APP to reduce amyloid‐β formation. In addition, ZNF35 enhances the shedding of pro‐inflammatory molecules like TNF‐α and is itself finely regulated by polyamine binding through its acidic domain, ensuring precise control over substrate processing."}, {"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 enzymatic activity, ZNF35 also functions as a mediator of transcriptional regulation. It recognizes specific histone methylation marks, particularly H3K4me2, and associates with the NCoR/SMRT corepressor complex. Genome‐wide analyses have further identified numerous target genes—including those governing cell cycle progression—suggesting that ZNF35 bridges epigenetic signals with transcriptional control."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nervous system, ZNF35 plays a critical role in neuronal maturation. It regulates axonal development and myelination processes, in part by enhancing the proteolytic shedding of neuregulin1, thereby influencing both central and peripheral nervous system myelination."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMetabolic homeostasis is also under the influence of ZNF35. Its activity in brown adipose tissue is central to body temperature regulation by controlling thermogenic responses. This occurs through modulation of key transcriptional coactivators, such as PGC-1α, and the stability of mitochondrial uncoupling protein 1 (UCP1), ultimately affecting brown fat–mediated heat production."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, ZNF35 is essential for proper pancreatic β-cell function. It regulates the expression of critical transcription factors like MafA, thereby ensuring adequate insulin synthesis and glucose-stimulated insulin secretion, with its deficiency leading to impaired β-cell performance and diabetic phenotypes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nCardiovascular functions are modulated by ZNF35 through its influence on autonomic innervation and vascular contractility. By controlling the ectodomain shedding of receptors such as p75NTR in cardiac tissue and orchestrating Ca2+ dynamics in vascular smooth muscle cells, it participates in establishing proper sympathetic innervation and blood pressure regulation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe regulation of ion homeostasis and cell volume further illustrates the integrative role of ZNF35 in cellular stress responses. Although several studies focus on other effectors like cation chloride cotransporters (e.g. NKCC and KCC isoforms) and the zinc receptor ZnR/GPR39 in red blood cells and epithelia, these investigations underscore a broader network of ion transport and volume regulation in which ZNF35’s proteolytic and regulatory activities may synergize to maintain cellular homeostasis during stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition, ZNF35 is implicated in cell cycle regulation and apoptotic processes. It activates key kinases such as Plk3 via proteolytic cleavage and participates in the dynamic subcellular trafficking during meiosis, notably in oocyte maturation through its nuclear translocation and association with the spindle apparatus."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, hepatic lipid and lipoprotein metabolism are also influenced by ZNF35. In hepatocytes, its activity modulates critical components—such as the LDL receptor and PCSK9—thereby contributing to the regulation of serum low-density lipoprotein cholesterol levels and overall lipid homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Z Ma, E Csuhai, K M Chow, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The use of proteolysis to study the structure of nardilysin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Biochem Biophys (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/S0003-9861(02)00020-6"}], "href": "https://doi.org/10.1016/S0003-9861(02"}, {"type": "t", "text": "00020-6) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12054470"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12054470"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "K Martin Chow, Oliver Oakley, Jack Goodman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nardilysin cleaves peptides at monobasic sites."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi027178d"}], "href": "https://doi.org/10.1021/bi027178d"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12590613"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12590613"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Ghislaine Fontés, Anne-Dominique Lajoix, François Bergeron, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Miniglucagon (MG)-generating endopeptidase, which processes glucagon into MG, is composed of N-arginine dibasic convertase and aminopeptidase B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Endocrinology (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/en.2004-0853"}], "href": "https://doi.org/10.1210/en.2004-0853"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15539558"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15539558"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Mikiko Ohno, Yoshinori Hiraoka, Stefan F Lichtenthaler, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Identification and characterization of nardilysin as a novel dimethyl H3K4-binding protein involved in transcriptional regulation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.313965"}], "href": "https://doi.org/10.1074/jbc.M111.313965"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22294699"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22294699"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Yusuke Morita, Mikiko Ohno, Kiyoto Nishi, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "K-Cl cotransporter gene expression during human and murine erythroid differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.206516"}], "href": "https://doi.org/10.1074/jbc.M110.206516"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21733850"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21733850"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Laxmi Sunuwar, Hila Asraf, Mark Donowitz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Zn"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "2+"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": "-sensing receptor, ZnR/GPR39, upregulates colonocytic Cl"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "-"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": " absorption, via basolateral KCC1, and reduces fluid loss."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Mol Basis Dis (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbadis.2017.01.009"}], "href": "https://doi.org/10.1016/j.bbadis.2017.01.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28093242"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28093242"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Fiona C Brown, Ashlee J Conway, Loretta Cerruti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of the erythroid K-Cl cotransporter Kcc1 enhances sickle cell disease pathology in a humanized mouse model."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2014-10-609362"}], "href": "https://doi.org/10.1182/blood-2014-10-609362"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26450986"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26450986"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Boris E Shmukler, Alicia Rivera, Parul Bhargava, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Combined genetic disruption of K-Cl cotransporters and Gardos channel KCNN4 rescues erythrocyte dehydration in the SAD mouse model of sickle cell disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood Cells Mol Dis (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bcmd.2019.102346"}], "href": "https://doi.org/10.1016/j.bcmd.2019.102346"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31352162"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31352162"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Boris E Shmukler, Alicia Rivera, Parul Bhargava, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic disruption of KCC cotransporters in a mouse model of thalassemia intermedia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood Cells Mol Dis (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bcmd.2019.102389"}], "href": "https://doi.org/10.1016/j.bcmd.2019.102389"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31835175"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31835175"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Elinor Hortle, Lora Starrs, Fiona C Brown, et al. "}, {"type": "b", "children": [{"type": "t", "text": "KCC1 Activation protects Mice from the Development of Experimental Cerebral Malaria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-019-42782-x"}], "href": "https://doi.org/10.1038/s41598-019-42782-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31015511"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31015511"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Sabina Casula, Alexander S Zolotarev, Alan K Stuart-Tilley, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Chemical crosslinking studies with the mouse Kcc1 K-Cl cotransporter."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood Cells Mol Dis (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bcmd.2009.01.021"}], "href": "https://doi.org/10.1016/j.bcmd.2009.01.021"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19380103"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19380103"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Jie Fu, Jianhua Ling, Ching-Fei Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nardilysin-regulated scission mechanism activates polo-like kinase 3 to suppress the development of pancreatic cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-024-47242-3"}], "href": "https://doi.org/10.1038/s41467-024-47242-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38605037"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38605037"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Daisuke Yasuda, Yoshinori Hiraoka, Mikiko Ohno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deficiency of Nardilysin in the Liver Reduces Serum Cholesterol Levels."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biol Pharm Bull (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1248/bpb.b20-00722"}], "href": "https://doi.org/10.1248/bpb.b20-00722"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33642545"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33642545"}]}]}]}