{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRIM16 is a multifunctional protein with a unique structure that lacks a classical RING domain yet harbors B‐box motifs capable of adopting RING‐like folds, endowing it with E3 ubiquitin ligase activity as demonstrated by its auto‐polyubiquitination function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, TRIM16 acts as a critical mediator of selective autophagy. It partners with Galectin‐3 to sense membrane damage, thereby coordinating the recruitment of core autophagy regulators (ULK1, Beclin 1, ATG16L1) to damaged endomembranes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Under stress conditions, TRIM16 plays an integral role in the formation and subsequent autophagic degradation of protein aggregates by stabilizing NRF2 via the p62–KEAP1–NRF2 complex."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Moreover, emerging evidence indicates that TRIM16 influences differentiation processes—such as osteogenic differentiation of mesenchymal stem cells through autophagy modulation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "—and regulates secretory autophagy, for instance by facilitating IL‐1β secretion under oxidative stress conditions implicated in disc degeneration."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Finally, TRIM16 has been shown to participate in lysophagy to remove damaged lysosomes, a function relevant in the maintenance of cellular homeostasis in chronic pulmonary disease."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, TRIM16 exerts potent tumor‐suppressor activities across a spectrum of malignancies. In neuroblastoma, it interacts with cytoplasmic vimentin and nuclear E2F1 to reduce cell motility and replication"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ", while in breast and neuroblastoma cells its binding to caspase‐2 enhances apoptotic cell death."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Dynamic changes in TRIM16 expression and subcellular localization are associated with cell cycle regulation and differentiation, as evidenced by its upregulation during the G1 phase in neuroblastoma cells."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " In lung cancer, particularly non‐small cell lung carcinoma, TRIM16 suppresses epithelial–mesenchymal transition (EMT) and metastasis via ubiquitination of vimentin"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", a process that is further highlighted in melanoma where its restoration reduces migratory and proliferative capacities."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Additional studies show that TRIM16 stabilizes TDP43 to mediate repression of cell cycle regulatory proteins"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "and in ovarian cancer its overexpression inhibits invasion by suppressing Sonic hedgehog signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": " Its regulatory roles extend to thyroid papillary cancer, where TRIM16 expression correlates with hormone receptor pathways"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": ", and in esophageal squamous cell carcinoma TRIM16 degradation, mediated by RASSF6, contributes to tumor progression."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": " Furthermore, in lung adenocarcinoma, TRIM16 facilitates the polyubiquitination and degradation of vimentin, a process modulated by long noncoding RNAs"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": ", and in colorectal cancer, it directly binds to and ubiquitinates Snail to prevent EMT and metastasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": " Notably, controversial observations in gastric cancer have linked TRIM16 expression with disease progression"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": ", and its regulation by oncogenic long noncoding RNAs further underscores its significance as a prognostic marker."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Finally, alterations in noncoding RNA regulatory networks also affect cisplatin resistance in non‐small cell lung cancer by modulating TRIM16 expression"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": ", while its expression in breast cancer has been correlated with various clinicopathological parameters."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRecent studies in hepatocellular carcinoma (HCC) add further dimensions to TRIM16’s function. A missense variant in TRIM16 (E121D) enhances its capacity to bind β‐catenin and promote its K48‐linked ubiquitination, thereby suppressing Wnt/β‐catenin signaling and reducing HCC risk."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": " Conversely, TRIM16-mediated ubiquitination of NFκB inhibitor NFKBIZ appears to reduce apoptosis and contribute to sorafenib insensitivity in HCC."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Jessica L Bell, Alena Malyukova, Jessica K Holien, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0037470"}], "href": "https://doi.org/10.1371/journal.pone.0037470"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22629402"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22629402"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Santosh Chauhan, Suresh Kumar, Ashish Jain, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Dev Cell (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.devcel.2016.08.003"}], "href": "https://doi.org/10.1016/j.devcel.2016.08.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27693506"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27693506"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Kautilya Kumar Jena, Srinivasa Prasad Kolapalli, Subhash Mehto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TRIM16 controls assembly and degradation of protein aggregates by modulating the p62-NRF2 axis and autophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embj.201798358"}], "href": "https://doi.org/10.15252/embj.201798358"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30143514"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30143514"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Wen-Ting Chen, Fan Zhang, Xing-Qi Zhao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Galectin-3 and TRIM16 coregulate osteogenic differentiation of human bone marrow-derived mesenchymal stem cells at least partly via enhancing autophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Bone (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bone.2019.115059"}], "href": "https://doi.org/10.1016/j.bone.2019.115059"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31521826"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31521826"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Qiangqiang Zheng, Haotian Shen, Zongrui Tong, et al. 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