{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOTUB1 is a multifunctional deubiquitinating enzyme that not only catalyzes the cleavage of Lys48‐linked ubiquitin chains but also noncatalytically inhibits ubiquitin transfer by directly binding to E2 conjugating enzymes. Biochemical and structural studies have shown that OTUB1 discriminates among polyubiquitin linkages via unique bidentate binding interactions and allosteric regulation by free ubiquitin. In response to DNA double‐strand breaks and during TGF‑β signalling, OTUB1 is recruited to chromatin or active SMAD complexes—processes further enhanced by posttranslational modifications (e.g. phosphorylation by CK2) that promote its nuclear localization. These investigations underscore its critical role in mediating ubiquitin signalling by blocking further polyubiquitin chain formation without necessarily relying on its catalytic activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn a variety of cancer contexts, OTUB1 plays an oncogenic or tumor‐suppressive role by regulating the stability and activity of key cellular effectors. For example, OTUB1 suppresses ubiquitin chain formation on p53—by counteracting MDM2/MDMX‐dependent ubiquitination—to stabilize and activate p53 in response to DNA damage. In parallel, OTUB1 deubiquitinates and stabilizes several oncogenic factors such as FOXM1, Snail, activated RAS and the estrogen receptor, thereby promoting cell proliferation, epithelial–mesenchymal transition, and resistance to chemotherapy in cancers such as colorectal, thyroid, glioma, melanoma and pancreatic carcinomas. Moreover, OTUB1 modulates additional substrates (e.g. DEPTOR, MSH2, RACK1) that impact mTOR signalling and genomic stability, highlighting its broad impact on cancer signalling pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOTUB1 itself is intricately regulated by various posttranslational modifications and protein–protein interactions that refine its activity in innate immunity and cellular homeostasis. 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