An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

The family of high mobility group box (HMGB) proteins participates in various biological processes including immunity, inflammation, as well as cancer formation and progression. However, its role in thyroid cancer remains to be clarified. We performed quantitative RT-PCR (qRT-PCR), western blot, enzyme-linked immunosorbent, immunohistochemistry, and immunofluorescence assays to evaluate the expression level and subcellular location of HMGB3. The effects of HMGB3 knockdown on malignant biological behaviors of thyroid cancer were determined by cell proliferation assays, cell cycle and apoptosis assays, and transwell chamber migration and invasion assays. Differential expression genes (DEGs) altered by HMGB3 were analyzed using the Ingenuity Pathway Analysis (IPA) and TRRUST v2 database. HMGB3 correlated pathways predicted by bioinformatic analysis were then confirmed using western blot, co-immunoprecipitation, dual-luciferase reporter assay, and flow cytometry. We found that HMGB3 is overexpressed and its downregulation inhibits cell viability, promotes cell apoptosis and cell cycle arrest, and suppresses cell migration and invasion in thyroid cancer. In PTC, both tissue and serum levels of HMGB3 are elevated and are correlated with lymph node metastasis and advanced tumor stage. Mechanistically, we observed the translocation of HMGB3 in PTC, induced at least partially by hypoxia. Cytoplasmic HMGB3 activates nucleic-acid-mediated TLR3/NF-κB signaling and extracellular HMGB3 interacts with the transmembrane TREM1 receptor in PTC. This study demonstrates the oncogenic role of HMGB3 cytoplasmic and extracellular translocation in papillary thyroid cancers; we recommend its future use as a potential circulating biomarker and therapeutic target for PTC.

The family of high mobility group box (HMGB) proteins participates in various biological processes including immunity, inflammation, as well as cancer formation and progression. However, its role in thyroid cancer remains to be clarified. We performed quantitative RT-PCR (qRT-PCR), western blot, enzyme-linked immunosorbent, immunohistochemistry, and immunofluorescence assays to evaluate the expression level and subcellular location of HMGB3. The effects of HMGB3 knockdown on malignant biological behaviors of thyroid cancer were determined by cell proliferation assays, cell cycle and apoptosis assays, and transwell chamber migration and invasion assays. Differential expression genes (DEGs) altered by HMGB3 were analyzed using the Ingenuity Pathway Analysis (IPA) and TRRUST v2 database. HMGB3 correlated pathways predicted by bioinformatic analysis were then confirmed using western blot, co-immunoprecipitation, dual-luciferase reporter assay, and flow cytometry. We found that HMGB3 is overexpressed and its downregulation inhibits cell viability, promotes cell apoptosis and cell cycle arrest, and suppresses cell migration and invasion in thyroid cancer. In PTC, both tissue and serum levels of HMGB3 are elevated and are correlated with lymph node metastasis and advanced tumor stage. Mechanistically, we observed the translocation of HMGB3 in PTC, induced at least partially by hypoxia. Cytoplasmic HMGB3 activates nucleic-acid-mediated TLR3/NF-κB signaling and extracellular HMGB3 interacts with the transmembrane TREM1 receptor in PTC. This study demonstrates the oncogenic role of HMGB3 cytoplasmic and extracellular translocation in papillary thyroid cancers; we recommend its future use as a potential circulating biomarker and therapeutic target for PTC.

An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

SummaryThismetadata record provides details of the data supporting the claims of therelated manuscript: “Synergistic activation of mutant TERTpromoter by Sp1 and GABPA in BRAFV600E-driven human cancers”.Thedata consist of 31 Excel .xlsx format spreadsheets and a Word .docx document.Therelated study tested the hypothesis that activated extracellularsignal-regulated kinase (ERK) may be recruited to mutant telomerase reversetranscriptase (TERT) promoter by pioneer transcription factors. DataaccessThe31 Excel .xlsx spreadsheets underlie the figures in the related manuscript, andare named according to the figure and subfigure they underlie (e.g., Figure 1B1.xlsx). These are openly available and are included together with this metadata record, and they contain data concerning qRT-PCR, dual-luciferase reporter assay, ChIP and TRAP assays described in the related manuscript. The sequence homology analsysis (underlyingSupplementary Figure 8) is openly available and is also included together with thismetadata record. Data for the Co-IP assay supporting Figure 3 are in the file WB-CoIPs.tiff and are available upon request to the corresponding author, Prof. Peng Hou: [email protected].

SummaryThismetadata record provides details of the data supporting the claims of therelated manuscript: “Synergistic activation of mutant TERTpromoter by Sp1 and GABPA in BRAFV600E-driven human cancers”.Thedata consist of 31 Excel .xlsx format spreadsheets and a Word .docx document.Therelated study tested the hypothesis that activated extracellularsignal-regulated kinase (ERK) may be recruited to mutant telomerase reversetranscriptase (TERT) promoter by pioneer transcription factors. DataaccessThe31 Excel .xlsx spreadsheets underlie the figures in the related manuscript, andare named according to the figure and subfigure they underlie (e.g., Figure 1B1.xlsx). These are openly available and are included together with this metadata record, and they contain data concerning qRT-PCR, dual-luciferase reporter assay, ChIP and TRAP assays described in the related manuscript. The sequence homology analsysis (underlyingSupplementary Figure 8) is openly available and is also included together with thismetadata record. Data for the Co-IP assay supporting Figure 3 are in the file WB-CoIPs.tiff and are available upon request to the corresponding author, Prof. Peng Hou: [email protected].

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