{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUSP28 is a ubiquitin‐specific protease that plays a central role in stabilizing key oncoproteins and transcription factors. It counteracts ubiquitin‐dependent degradation—most notably, it deubiquitinates and thereby stabilizes MYC, c‐JUN, NOTCH1, LSD1, FOXM1, and ΔNp63—thus fostering cellular proliferation and tumor growth in a variety of cancers such as colon, breast, glioma, intestinal malignancies, and neuroblastoma. In many of these contexts, USP28 acts in opposition to the E3 ligase FBW7, which normally earmarks these substrates for proteasomal degradation."}, {"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": "\nIn addition to promoting oncogene stability, USP28 contributes to the cellular response to DNA damage and mitotic stress. By working in concert with the DNA damage mediator 53BP1 and checkpoint kinases such as Chk2, USP28 facilitates the stabilization and activation of p53, particularly during centrosome loss or prolonged mitosis. Through this 53BP1–USP28–p53 axis, cells are able to enforce appropriate cell cycle arrests in response to genotoxic or mitotic challenges, thereby maintaining genomic integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, USP28 extends its functional repertoire by regulating additional substrates that impact angiogenesis, tumor metabolism, and therapeutic resistance. It has been shown to antagonize degradation of HIF‑1α, modulate the stability of LSD1 and UCK1, and stabilize STAT3 to influence processes such as angiogenesis and the cellular response to chemotherapeutics. Structural studies further reveal that USP28 functions as an active dimer—and that its activity can be modulated by interactions with endogenous factors and microRNAs (for example, miR‑4295 and miR‑216b) as well as by small‐molecule inhibitors (including vismodegib). These aspects of USP28 biology contribute to its roles in drug resistance mechanisms (for instance, via MAST1 stabilization leading to cisplatin resistance), and underscore its potential as a therapeutic target across multiple tumors including non‐small cell lung cancer, hepatocellular carcinoma, triple‐negative breast cancer, and even non‐malignant conditions such as polycystic kidney disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Nikita Popov, Michael Wanzel, Mandy Madiredjo, et al. 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