STAU1 exhibits oncogenic characteristics and modulates alternative splicing and gene expression in A549 lung adenocarcinoma cells
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1175565 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| SRR31057910_1.fastq.gz | Fastqsanger.gz | |||
| SRR31057910_2.fastq.gz | Fastqsanger.gz | |||
| SRR31057911_1.fastq.gz | Fastqsanger.gz | |||
| SRR31057911_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 5 |
Similar Datasets
Project description:Staufen double-stranded RNA-binding protein 1 (STAU1) assumes a significant role in cancer development and is correlated with survival outcomes in patients with lung cancer. Nevertheless, its specific functions and molecular mechanisms in lung adenocarcinoma (LUAD) remain insufficiently explored. In our research, we established a STAU1 knockdown expression model within the A549 cell line. We discerned that the knockdown of STAU1 significantly suppressed the proliferation, invasion, and migration of A549 cells and enhanced the level of cell apoptosis. Through RNA-seq analysis, we identified 197 differentially expressed genes (DEGs) and 1,362 STAU1-Regulated alternative splicing Events (ASEs). The DEGs were specifically enriched in cell adhesion pathways, while the ASE genes were mainly associated with cell division and the cell cycle. Our study implies that STAU1 possesses oncogenic characteristics and may modulate DEGs and ASEs to affect the proliferation, invasion, and migration of A549 cells. This research provides novel insights that might contribute to the diagnosis and treatment of LUAD.
2025-05-29 | GSE279930 | GEO
Project description:To study the potential targets and functions of STAU1 which might be related to neuropathic pain, we obtained STAU1-regulated transcriptome in HeLa cells. High-throughput RNA sequencing(RNA-seq) were performed for HeLa cells and control cells to define the comprehensive gene expression profiles and identify the genome-wide alternative splicing events regulated by STAU1.
2020-10-20 | GSE136890 | GEO
Project description:Monosome and disome profiling was performed on Flag-STAU1 Flp-In 293 T-REx to study the causes of ribosomal collisions, and whether this may be modulated by the presence/absence of Staufen-1. Cells were treated with either an siRNA targeting STAU1 transcript (4x samples) or a control siRNA (2x samples). Two of the four samples treated with the STAU1 siRNA had siRNA-resistant STAU1 mRNA expression induced by doxycycline (rescue). Sequencing libraries from monosome and disome fractions were generated in parallel from the same samples. Note that unique molecular identifiers/random barcodes (UMIs/RBCs) were included in the sequencing experiment. Each UMI has been moved to the fastq read name of each read. For example \\"xxxxxxrbc:AGCCAAT\\" in the read name signifies that the given read had a UMI of \\"AGCCAAT\\". Using these UMIs, PCR duplicates can be removed with UMI-Tools following read alignment.
2023-04-30 | E-MTAB-9669 | biostudies-arrayexpress
Project description:Cancer development is regulated by inflammation. Staufen 1 (STAU1) is an RNA-binding protein whose expression level is critical in cancer cells as it is related to cell proliferation or cell death. STAU1 expression levels are downregulated during mitosis due to its degradation by the E3 ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C). In this paper, we map the molecular determinant involved in STAU1 degradation in mitosis to amino acids 38-50 and, by alanine scanning, we shorten the motif to F39PxPxxLxxxxL50 (FPL-motif). Mutation of the FPL-motif prevents STAU1 degradation by APC/C. Interestingly, a search in databases reveals that the FPL-motif is shared by 15 additional proteins most of them being involved in inflammation. We show that one of these proteins, MAP4K1, is indeed degraded via the FPL-motif; however, it is not a target of APC/C. Using proximity labeling with STAU1, we identify TRIM25, an E3-ubiquitin ligase involved in the innate immune response and interferon production, as responsible for STAU1 and MAP4K1 degradation, dependent on the FPL-motif. These results are consistent with previous studies that linked STAU1 to cancer-induced inflammation and identify a novel degradation motif that likely coordinates a novel family of proteins involved in inflammation.
2023-03-11 | PXD036675 | Pride
Project description:Cancer development is regulated by inflammation. Staufen 1 (STAU1) is an RNA-binding protein whose expression level is critical in cancer cells as it is related to cell proliferation or cell death. STAU1 expression levels are downregulated during mitosis due to its degradation by the E3 ubiquitin ligase anaphase-promoting complex/cyclosome (APC/C). In this paper, we map the molecular determinant involved in STAU1 degradation in mitosis to amino acids 38-50 and, by alanine scanning, we shorten the motif to F39PxPxxLxxxxL50 (FPL-motif). Mutation of the FPL-motif prevents STAU1 degradation by APC/C. Interestingly, a search in databases reveals that the FPL-motif is shared by 15 additional proteins most of them being involved in inflammation. We show that one of these proteins, MAP4K1, is indeed degraded via the FPL-motif; however, it is not a target of APC/C. Using proximity labeling with STAU1, we identify TRIM25, an E3-ubiquitin ligase involved in the innate immune response and interferon production, as responsible for STAU1 and MAP4K1 degradation, dependent on the FPL-motif. These results are consistent with previous studies that linked STAU1 to cancer-induced inflammation and identify a novel degradation motif that likely coordinates a novel family of proteins involved in inflammation.
2023-02-21 | PXD037703 | Pride
Project description:Alterations in cellular antigen processing and presenting machinery has gained increased interest as a hallmark of cancer-related inflammation. Growing evidence suggest that proteasome composition and immunoproteasome expression can influence antigen processing. By performing immunopeptidomics on A549 lung adenocarcinoma cell line following depletion of proteasome regulator PSME4 we identified alterations in the antigenic landscape resulting from changes in proteasome processing.
2023-03-30 | PXD037365 | Pride
Project description:Alterations in cellular antigen processing and presenting machinery has gained increased interest as a hallmark of cancer-related inflammation. Growing evidence suggest that proteasome composition and immunoproteasome expression can influence antigen processing. By performing immunopeptidomics on A549 lung adenocarcinoma cell line following depletion of proteasome regulator PSME4 we identified alterations in the antigenic landscape resulting from changes in proteasome processing.
2023-03-30 | PXD028364 | Pride
Project description:hiCLIP protocol was followed to isolate RNA bound to 3XFLAG-STAU1 protein and amplify cDNA library as described in the manuscript. Specific barcodes were used for each RT reaction, and are specified below for each sequencing run. Random barcodes were also incoperated into cDNAs to distinguish between PCR duplication of cDNA products. The final products were obtained by PCR with Illumina paired-end sequencing primers: 5-CAAGCAGAAGACGGCATACGAGATCGGTCTCGGCATTCCTGCTGAACCGCTCTTCCGATCT-3; 5-AATGATACGGCGACCACCGAGATCTACACTCTTTCCCTACACGACGCTCTTCCGATCT-3
2015-03-02 | E-MTAB-2937 | biostudies-arrayexpress
Project description:Purpose of the study was to investigate the impact of reducing the efficiency of minor (U12-type) splicing on the growth and gene expression of a human cancer cell line. We chose the A549 cell line, derived from a human lung adenocarcinoma, for this study. There are only approximately 700 genes (3.5%) in the human genome that contain a minor intron. Most transcripts (96.5%) require only major (U2-dependent) splicing for correct gene expression. This is carried out by the major spliceosome. A different spliceosome, known as the minor or U11/12-type spliceosome, is required to excise minor introns from pre-RNA transcripts that contain them. One of the unique protein components of the minor spliceosome is a 65kDa protein encoded by the RNPC3 gene. To reduce the efficiency of minor splicing, we used siRNA knockdown methodology to deplete RNPC3 transcripts in A549 cells by approximately 70%. Specifically, A549 cells in growth phase were transfected with siRNA targeted to RNPC3 transcripts for 72h. Control A549 cells were treated in the same experiment with non-targeted (NT) siRNA molecules instead of siRNA targeted to RNPC3.
2025-06-03 | GSE190943 | GEO