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Next-generation sequencing analysis of 7-month-old SRSF2 flox/flox and SRSF2-PKO mice pancreatic islet transcriptome

ABSTRACT: We report insulin secretion defects in SRSF2 Ins2-Cre mice, in which SRSF2 is ablated in pancreatic β cells.

ORGANISM(S): Mus musculus

PROVIDER: GSE175969 | GEO | 2024/04/28

REPOSITORIES: GEO

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Next Generation Sequencing Analysis of SRSF1 flox/flox and SRSF1-KO pancreatic islet Transcriptome

Project description:we report insulin secretion defects in SRSF1 Ins2-Cre mice, in which SRSF1 is ablated in pancreatic β cells.

2023-04-17 | GSE173455 | GEO

Next Generation Sequencing Analysis of Wild Type and SRSF2-MKO Skeletal Muscle Transcriptomes

Project description:We report skeletal muscle developmental defects in SRSF2 MyoD-Cre mice, in which SRSF2 is ablated in skeletal muscle.

2023-06-02 | GSE151946 | GEO

Next Generation Sequencing Analysis of Wild Type and SRSF2-/- 5 month mice liver Transcriptomes

Project description:We generated the liver specific SRSF2 -/- mice, and collected their liver at 5 month after born and controls. Then, we extracted RNAs and performed next generation sequencing. By comparing sequcing data from WT and SRSF2 -/- samples, we profiled the alternative splicing events and gene expression regulated by SRSF2 during mouse liver development process.

2019-07-31 | GSE85041 | GEO

Next Generation Sequencing Analysis of control and SRSF2-/- Huh7 cells Transcriptomes

Project description:We generated the SRSF2-/- Huh7 cells,and collected the cells at 2 days after transfected with siRNA. Then, we extracted RNAs and performed next generation sequencing. By comparing sequencing data from control and SRSF2 -/- samples, we profiled the alternative splicing events and gene expression regulated by SRSF2 in HCC.

2017-01-17 | GSE78705 | GEO

Next Generation Sequencing Analysis of Wild Type and SRSF2-/- D11 mice liver Transcriptomes

Project description:We generated the liver specific SRSF2 -/- mice, and collected their liver at 11 day after birth and controls. Then, we extracted RNAs and performed next generation sequencing. By comparing sequencing data from WT and SRSF2 -/- samples, we profiled the alternative splicing events and gene expression regulated by SRSF2 during mouse liver development process.

2016-04-19 | GSE73536 | GEO

SRSF2 mutations impair hematopoiesis and alter exon recognition

Project description:Mutations within genes encoding spliceosomal proteins are the most common class of mutations in patients with myelodysplastic syndromes, yet it is currently not well understood how these mutations impact hematopoiesis or RNA splicing. Here we report that mutations affecting the splicing factor SRSF2 alter its normal RNA recognition activity, resulting in impaired hematopoietic differentiation and myelodysplasia. Commonly occurring SRSF2 mutations impaired wildtype SRSF2’s normal RNA-binding avidity and preference for specific exonic splicing enhancer RNA motifs. Integration of murine and human transcriptome data identified recurrent mis-splicing of key transcriptional regulators in the presence of mutant SRSF2, including promotion of a highly conserved “poison” exon of EZH2 that results in nonsense-mediated decay and contributes to impaired hematopoiesis. These data provide a mechanistic basis for the enrichment of specific mutations in spliceosomal proteins in myelodysplasia, and suggest that altered RNA recognition activity is a novel mechanism of leukemogenesis. mRNA profiles of murine model and K562 cells expressing SRSF2 WT, mutants and knockdown of SRSF2 in TF-1 cells generated by deep sequencing.

2015-05-12 | E-GEOD-65349 | biostudies-arrayexpress

Disease-associated mutation in SRSF2 misregulates splicing by altering RNA binding affinities

Project description:SRSF2 is an RNA binding protein that plays important roles in splicing of mRNA precursors. Mutations in SRSF2 are frequently found in patients with myelodysplastic syndromes and certain leukemias, but how they affect SRSF2 function has only begun to be examined. Here we used CRISPR/Cas9 to introduce the P95H mutation to SRSF2 in K562 leukemia cells, generating an isogenic model so that splicing alterations can be attributed solely to mutant SRSF2. We found that SRSF2 (P95H) misregulates 548 splicing events (<1% of total). Of these, 374 involve the inclusion of cassette exons, and the inclusion was either increased (206) or decreased (168). We detected a specific motif (UCCA/UG) enriched in the more included exons and a distinct motif (UGGA/UG) in the more excluded exons. RNA gel shift assays showed that a mutant SRSF2 derivative bound more tightly than its wild-type counterpart to RNA sites containing UCCAG, but less tightly to UGGAG sites. The pattern of exon inclusion or exclusion thus correlated in most cases with stronger or weaker RNA binding, respectively. We further show that the P95H mutation does not affect other functions of SRSF2, i.e., protein-protein interactions with key splicing factors. Our results thus demonstrate that the P95H mutation positively or negatively alters the binding affinity of SRSF2 for cognate RNA sites in target transcripts, leading to misregulation of exon inclusion. Our findings not only shed light on the mechanism of the disease-associated SRSF2 mutation in splicing regulation, but also reveal a group of mis-spliced mRNA isoforms for potential therapeutic targeting. Examination of differentially spliced events in K562 CRISPR cell clones (with wild-type or mutant SRSF2) by RNA sequencing

2015-08-10 | E-GEOD-71299 | biostudies-arrayexpress

Targeting mitophagy in SRSF2 mutant hematologic malignancies

Project description:Recurrent Glycogen synthase kinase-3 (GSK-3) phosphorylates multiple splicing factors, including SRSF2, and regulates the splicing of a broad range of mRNAs in human cells. Inhibition of GSK-3 disrupts splicing and promotes cell death in hematopoietic cells with heterozygous mutations in SRSF2 and not in cells with wild-type splicing factors. To characterize how GSK-3 inhibition alters the cellular proteome in SRSF2-P95H/+ cells, we have performed quantitative mass spectrometry (qMS) on K562 cells with SRSF2P95H/+ knocked into the endogenous locus (PMID 30799057) and parental K562 cells, treated with the GSK-3 inhibitor CHIR99021. We focused on the mitochondrial proteome using human proteome (UniprotKB) and mitochondrial (MitoCarta 3.0) databases for protein identification, identifying 163 mitochondrial proteins whose levels are affected by SRSF2 mutation.

2024-06-22 | PXD043213 | Pride

Next Generation Sequencing Analysis of Gene expression of wild-type AGS cells and AGS cells transfected with an siRNA targeting SRSF2

Project description:SRSFs are a subset of RNA binding proteins that exert precise control over RNA splicing, including cancer-associated AS events. Serine/arginine-rich splicing factors 2 (SRSF2), a member of SRSF family, plays a crucial role in regulating splicing events. We profiled gene expression and splicing changes in AGS cells silencing SRSF2. Our study unveils that SRSF2 binds to the exon 4 region of YTHDF1 pre-mRNA, inducing YTHDF1Δexon 4 skipping and resulting in elevation levels of the oncogenic YTHDF1-S in GC. Overall, we provide evidence that YTHDF1 is an AS target of SRSF2.

2024-06-26 | GSE270390 | GEO

SRSF2 is essential for hematopoiesis and its myelodysplastic syndromes-related mutations dysregulate alternative pre-mRNA splicing

Project description:We report the biological function of Srsf2 in hematopoiesis in conditional knockout mouse models. Ablation of Srsf2 in the hematopoietic lineage caused embryonic lethality, and Srsf2-deficient fetal liver cells showed significantly enhanced apoptosis and decreased hematopoietic stem/progenitor cells. Induced ablation of Srsf2 in adult Mx1Cre/ Srsf2flox/flox mice upon polyinosinic:polycytidylic acid injection demonstrated a significant decrease in lineage-/Sca+/cKit+ cells in bone marrow. To reveal the functional impact of MDS-associated mutations in SRSF2, we profiled global splicing responses on an MDS-L cell line using RASL-seq, and found that the P95H missense mutation and P95 to R102 in-frame 8 amino-acid deletion caused significant changes in alternative splicing. The affected genes were enriched in cancer development and apoptosis. These findings suggest that intact Srsf2 is essential for the functional integrity of the hematopoietic system, and its mutations are likely key driver events to MDS. MDS-L cells (in triplicate) were transfected by srsf2 shRNA only, or pTRIPZ vectors containing both srsf2 shRNA and srsf2 mutants cDNA including P95H and P95 8 amino acid deletion as well as wild-type construct, followed by Dox induction. Total RNAs were extracted and been analyzed by RASL-seq.

2015-03-01 | E-GEOD-61052 | biostudies-arrayexpress

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