Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

RBM15-mediated Metabolic Reprogramming Boosts Immune Response in Colorectal Cancer

ABSTRACT: RBM15-mediated Metabolic Reprogramming Boosts Immune Response in Colorectal Cancer

PROVIDER: PRJNA1174067 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR31023779_1.fastq.gz	Fastqsanger.gz
	SRR31023779_2.fastq.gz	Fastqsanger.gz
	SRR31023780_1.fastq.gz	Fastqsanger.gz
	SRR31023780_2.fastq.gz	Fastqsanger.gz
	SRR31023781_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 12

Similar Datasets

RBM15-mediated Metabolic Reprogramming Boosts Immune Response in Colorectal Cancer

Project description:Immune checkpoint blockade (ICB) offers therapeutic options for patients with advanced colorectal cancer; however, only a subset of patients with microsatellite instability-high (MSI-H) tumors respond to treatment. Therefore, strategies to enhance immunotherapy sensitivity are urgently needed. In this study, we demonstrate that RBM15 is highly expressed in colorectal cancer and is associated with poor prognosis. Loss of RBM15 increases the expression of fumarate hydratase (FH), leading to a reduction in its substrate fumarate, which acts as a suppressor of anti-tumor immunity. Notably, RBM15 depletion delays tumor growth by promoting CD8+ T cell infiltration. Our findings identify RBM15 as a key suppressor of anti-tumor immunity, suggesting that targeting RBM15 could be a promising therapeutic strategy in colorectal cancer.

2025-04-15 | GSE279678 | GEO

Indole-3-lactic acid suppresses colorectal cancer via metabolic reprogramming

Project description:Indole-3-lactic acid suppresses colorectal cancer via metabolic reprogramming

| PRJNA1133650 | ENA

Rbm15-irCLIP-seq

Project description:Rbm15-irCLIP-seq

| PRJNA647279 | ENA

Rbm15-irCLIP-seq

Project description:we performed infrared crosslinking immunoprecipitation followed by sequencing (irCLIP-seq) (Zarnegar et al., 2016) for Rbm15 to directly map its binding sites on RNA. As a principle of concept, the cells were engineered to simultaneously express emGFP-Rbm15 and Xist RNA together, as Rbm15 strongly interacts with Xist A-repeat to deposit the m6A methylation downstream. Cross-linking induced truncation site (CITS or RT stops) is the main signature occurring at our irCLIP-seq datasets. RNA meta-profile plot against normalized transcripts shows that these CITSs reside across the transcript, with 2 main peaks in transcript starts and near the stop-codon regions, in agreement with the RBM15/15B binding profile in human cells (Patil et al., 2016).Motif analysis against CITSs revealed that Rbm15 binding sites prefer U-rich stretches, namely 3 or 4 consecutive Us. This is also true for crosslinking induced mutations (CIMS).

2020-09-15 | GSE154708 | GEO

RBM15 CoIP in mouse Embryonic Stem cells

Project description:RBM15 interactome has been determined in mouse Embryonic Stem cells. The cells express inducible emGFP-PreScission-RBM15 alongside with inducible Xist RNA.

2020-02-07 | PXD017348 | Pride

PSY Suppresses Colorectal Cancer Progression by Targeting Oncogenic Signaling and Metabolic Reprogramming

Project description:PSY Suppresses Colorectal Cancer Progression by Targeting Oncogenic Signaling and Metabolic Reprogramming

| PRJNA1206761 | ENA

Oncogenic KRAS and BRAF drive metabolic reprogramming in colorectal cancer JEH 2016

Project description:Multiplexed PRM analysis for metabolic reprogramming in isogenic cell lines with KRAS or BRAF mutations.

2016-02-01 | MSV000079486 | MassIVE

Control of gene expression by Ott1/RBM15 protein

Project description:The conserved mRNA nuclear export receptor NXF1 (Mex67 in yeast) assembles with messenger ribonucleoproteins (mRNP) in the nucleus and guides them through the nuclear pore complex (NPC) into the cytoplasm. The DEAD-box RNA helicase Dbp5 is essential for nuclear export of mRNA and is thought to dissociate Mex67 from mRNP upon translocation, thereby generating directional passage. However, the molecular mechanism by which Dbp5 recognizes Mex67-containing mRNP is not clear. Here we report that the human NXF1-binding protein RBM15 binds to DBP5 specifically and enables its direct contact with mRNA. We found that RBM15 is enriched at the nuclear envelope and colocalizes with DBP5 at the NPC. Knockout of RBM15’s orthologue in mouse (Ott1) leads to global changes in mRNA expression and excessive mRNA accumulation in the cytoplasm, indicating an essential role of RBM15 in mRNA export regulation. We propose that RBM15 acts locally at the NPC, by transiently bridging the NXF1-mRNP complexes to DBP5, thereby contributing to the substrate specificity of mRNA export.

2008-06-18 | GSE11785 | GEO

Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing

Project description:RBM15, an RNA binding protein, determines cell-fate specification of many tissues including blood. We demonstrate that RBM15 is methylated by protein arginine methyltransferase 1 (PRMT1) at residue R578 leading to its degradation via ubiquitylation by an E3 ligase (CNOT4). Overexpression of PRMT1 in acute megakaryocytic leukemia cell lines blocks megakaryocyte terminal differentiation by downregulation of RBM15 protein level. Restoring RBM15 protein level rescues megakaryocyte terminal differentiation blocked by PRMT1 overexpression. At the molecular level, RBM15 binds to pre-mRNA intronic regions of genes important for megakaryopoiesis such as GATA1, RUNX1, TAL1 and c-MPL. Furthermore, preferential binding of RBM15 to specific intronic regions recruits the splicing factor SF3B1 to the same sites for alternative splicing. Therefore, PRMT1 regulates alternative RNA splicing via reducing RBM15 protein concentration. Targeting PRMT1 may be a curative therapy to restore megakaryocyte differentiation for acute megakaryocytic leukemia.

2015-11-17 | GSE73893 | GEO