e2f1  (Genecopoeia)

Journal: Frontiers in Immunology

Article Title: Multi-omics analysis and functional validation reveal the oncogenic role of TRIP13

doi: 10.3389/fimmu.2026.1691436

Figure Lengend Snippet: E2F1 transcriptionally activates TRIP13 to drive Palbociclib resistance in prostate cancer. In TCGA prostate cancer, samples were stratified into high and low TRIP13 expression groups. Differential expression analysis was performed, followed by GSEA enrichment analysis. In the bubble plot, different colors represent NES values, while bubble sizes correspond to the log-adjusted P -values (A) . Spearman correlation plots showing the relationship between E2F1 and TRIP13, panels: (B) TCGA prostate cancer data, (C) PRAD_SU2C_2019 data. (D) Ominer network tool prediction of potential transcription factors for TRIP13. (E) Chip-Seq analysis of E2F1 binding to the TRIP13 promoter region from Chip-Atlas. (F) GPSAdb data indicate reduced TRIP13 expression following E2F1 knockdown. Different colors represent different LogFC. (G) PC-3 cells were transfected with specified shRNA for 72 hours, followed by puromycin selection. These cells were treated with collected for ChIP-qPCR analysis using IgG or E2F1 antibodies. Data represent the mean ± SEM from three independent experiments. ** indicates P < 0.01, *** indicates P < 0.001. (H, I) PC-3 and C4-2 cells were transfected with specified shRNA for 72 hours. After puromycin screening, cells were subjected to western blot analysis (H) and RT-qPCR assay (I) . Data represent the mean ± SEM from three independent experiments. ** indicates P < 0.01, *** indicates P < 0.001. (J, K) PC-3 and C4-2 cells were transfected with designated plasmids for 24 hours. Following puromycin screening, cells underwent western blot analysis (J) and RT-qPCR assay (K) . Data are presented as the mean ± SEM from three independent experiments. *** indicates P < 0.001. (L) The sequence and location of the E2F1 binding peak in the TRIP13 promoter. WT, wild type, MUT, mutant. (M) PC-3 cells were transfected with indicated plasmid for 24 h. After puromycin selection, the cells were harvested and the activity of the TRIP13 promoters was measured. Data are presented as the mean ± SEM from three independent experiments. ** indicates P < 0.01, ns, not significant. (N) PC-3 and C4-2 cells were transfected with specified shRNA for 72 hours and indicated plasmid for 24 h, followed by puromycin selection. The cells were then treated with incremental doses of palbociclib for 24 hours and subjected to CCK-8 assays. Data were expressed as the mean ± SEM and repeated three times. Statistical significance was determined using the indicated tests, with P <0.05 considered significant.

Article Snippet: OmicLinkTM Expression Clone (CMV Promoter) plasmids (Catalog #: EX-V0006-M14, GeneCopoeia, USA) were utilized to clone the cDNA of TRIP13 and E2F1 for their overexpression.

Techniques: Expressing, Quantitative Proteomics, ChIP-sequencing, Binding Assay, Knockdown, Transfection, shRNA, Selection, ChIP-qPCR, Western Blot, Quantitative RT-PCR, Sequencing, Mutagenesis, Plasmid Preparation, Activity Assay, CCK-8 Assay

Journal: Current Oncology

Article Title: E2F1-Driven WDHD1 Transcription Enhances Cell-Cycle Progression and Promotes Pancreatic Cancer Progression

doi: 10.3390/curroncol33040186

Figure Lengend Snippet: The E2F1–WDHD1 axis promotes malignant phenotypes in pancreatic cancer by upregulating cyclin D1. ( A , B ) Expression of cell cycle-related proteins after knocking down WDHD1. β-actin served as a loading control; Representative images were selected from three independent experiments. ( C ) Expression of CDK4 and cyclin D proteins after overexpression of WDHD1. β-actin served as a loading control. Representative images were selected from three independent experiments. ( D ) RNA expression levels of E2F1 in various pancreatic cancer cell lines show elevated expression compared to normal pancreatic cell lines ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 (Student’s t -test), ns, non-significant. ( E , F ) Overexpression of E2F1 can increase the expression of WDHD1 at both the RNA and protein levels ( n = 4 independent biological replicates). Summary statistics for each experimental group reported as means ± SD. Statistical significance: * p < 0.05, *** p < 0.001 (Student’s t -test). β-actin served as a loading control. Representative images were selected from three independent experiments. ( G ) The impact of WDHD1 knockdown after overexpression of E2F1 on cyclin D1, cyclin D3, and CDK4 at protein level. β-actin served as a loading control. Representative images were selected from three independent experiments. ( H ) E2F1 activates the WDHD1 promoter. E2F1 overexpression significantly increased the activity of a luciferase reporter driven by the full-length WDHD1 promoter relative to the vector control, consistent with direct transcriptional activation of WDHD1 by E2F1 ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: *** p < 0.001 (Student’s t -test). ( I ) ChIP–qPCR shows enrichment of the WDHD1 promoter in anti-E2F1 immunoprecipitates relative to IgG control ( n = 3 independent biological replicates). Summary statistics for each experimental group reported as means ± SD; Statistical significance: **** p < 0.0001 (Student’s t -test). The unedited blots can be found in .

Article Snippet: The antibodies utilized in this study included anti-WDHD1 (abclonal, A15396, 1:1000), anti-E2F1 (abclonal, A19579, 1:1000), anti-CDK4 (abclonal, A0366, 1:1000), anti-CDK6 (abclonal, A1545, 1:1000), anti-cyclin D1 (abclonal, A1301, 1:1000), and anti-cyclin D3 (abclonal, A3589, 1:1000). β-actin (ZSGB-BIO, TA-09, 1:1000) was used as the sample loading control.

Techniques: Expressing, Control, Over Expression, RNA Expression, Knockdown, Activity Assay, Luciferase, Plasmid Preparation, Activation Assay, ChIP-qPCR

Journal: bioRxiv

Article Title: “Targeting LARP1 Enhances Carboplatin Sensitivity and Suppresses Tumor Growth in Endometrial Cancer”

doi: 10.64898/2026.03.22.713473

Figure Lengend Snippet: (A, B) Kaplan–Meier plot showing that overexpression of E2F1 is associated with shorter overall survival (A) and progression-free interval (B) in endometrial cancer cohort. (C, D) Kaplan–Meier plot showing that co-overexpression of LARP1 and E2F1 is associated with shorter overall survival (C) and progression-free interval (D) in endometrial cancer cohort. (E) Spearman correlation analysis shows a correlation between LARP1 and E2F1 in endometrial cancer patients.

Article Snippet: Cells were then incubated overnight at 4 °C with the following primary antibodies: LARP1 (Cat. No. sc-515873; 1:200 dilution; Santa Cruz Biotechnology, Dallas, TX, USA) and E2F1 (Cat. No. 3742S; 1:400 dilution; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Over Expression

Journal: bioRxiv

Article Title: “Targeting LARP1 Enhances Carboplatin Sensitivity and Suppresses Tumor Growth in Endometrial Cancer”

doi: 10.64898/2026.03.22.713473

Figure Lengend Snippet: (A, B) Immunoblot analysis showing the protein expression of LARP1 and E2F1 after transfecting ISHI (A) and HEC-1A (B) cells with control or LARP1 siRNA. β-actin was used as a loading control. (C) Images representing immunofluorescence staining of LARP1 (green) and E2F1 (red) in HEC-1A cells after transfection with control or LARP1 siRNA. DAPI was used as a counter stain. Scale bar = 50 µm.

Article Snippet: Cells were then incubated overnight at 4 °C with the following primary antibodies: LARP1 (Cat. No. sc-515873; 1:200 dilution; Santa Cruz Biotechnology, Dallas, TX, USA) and E2F1 (Cat. No. 3742S; 1:400 dilution; Cell Signaling Technology, Danvers, MA, USA).

Techniques: Western Blot, Expressing, Control, Immunofluorescence, Staining, Transfection