{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUbiquitin‐specific protease 13 (USP13) is emerging as a multifaceted deubiquitinating enzyme that governs diverse aspects of cellular homeostasis. Several studies have shown that USP13 removes ubiquitin chains from key autophagy regulators such as Beclin1—thereby diminishing its degradation—and from p62, which enhances p62 oligomerization to facilitate selective autophagy and modulate antioxidant responses. In embryonic stem cells, USP13 also stabilizes signaling molecules (for example, Raf1) to influence pluripotency and differentiation, while its actions on TopBP1 and cohesin components help maintain proper replication stress responses and chromatin dynamics. Moreover, USP13 localizes to stress granules during heat shock, where it fine‐tunes ubiquitin turnover to control both the assembly and disassembly of these transient ribonucleoprotein complexes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the realm of cancer and other human diseases, USP13 plays a context‐dependent regulatory role by stabilizing or enhancing the activity of critical proteins. For instance, USP13 deubiquitinates and stabilizes the tumor suppressor PTEN—limiting PI3K/AKT pathway activation—yet in other contexts it preserves oncoproteins such as c‐Myc (thereby promoting glioblastoma stem cell self‐renewal and hepatocellular carcinoma proliferation), MCL1, and MITF (contributing to tumor growth in melanoma). USP13 also sustains metabolic reprogramming in ovarian cancer by targeting enzymes like ATP citrate lyase and oxoglutarate dehydrogenase, and it modulates the DNA damage response by deubiquitinating RAP80 and ensuring proper BRCA1 recruitment. Additional investigations have linked USP13 to the stabilization of cyclin D1 in gastric cancer, the preservation of METTL3 in osteosarcoma (with subsequent effects on autophagy via ATG5 mRNA), and the regulation of proteins like ZHX2 in renal carcinoma. Beyond cancer, altered USP13 activity has been implicated in neurodegenerative conditions by affecting the turnover of tau, parkin, and alpha‐synuclein, and it may also influence the immunological landscape in viral infections as well as the lineage determination programs in lung squamous cell carcinoma and prostate cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nCollectively, these findings underscore the pleiotropic roles of USP13—ranging from the regulation of autophagy, DNA repair, and chromatin organization to its context‐dependent stabilization of both tumor suppressors and oncoproteins. By fine‐tuning ubiquitin signaling, USP13 not only orchestrates key cellular processes essential for homeostasis but also drives metabolic reprogramming, proliferation, and survival in various cancers, while its dysregulation may contribute to neurodegenerative and inflammatory diseases. Such multifarious functions make USP13 a promising therapeutic target, with its inhibition (for example, by small molecules like spautin‑1 or 2‑methoxyestradiol) holding potential to enhance chemosensitivity and counteract disease progression across diverse clinical contexts.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Junli Liu, Hongguang Xia, Minsu Kim, et al. 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