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NONO-mediated alternative splicing of SETMAR inhibits lymphatic metastasis in bladder cancer

ABSTRACT: NONO-mediated alternative splicing of SETMAR inhibits lymphatic metastasis in bladder cancer

PROVIDER: PRJNA613734 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11362445_1.fastq.gz	Fastqsanger.gz
	SRR11362445_2.fastq.gz	Fastqsanger.gz
	SRR11362446_1.fastq.gz	Fastqsanger.gz
	SRR11362446_2.fastq.gz	Fastqsanger.gz
	SRR11362447_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

NONO-mediated alternative splicing of SETMAR inhibits lymphatic metastasis in bladder cancer

Project description:To explore the molecular mechanism underlying NONO-mediated lymphatic metastasis inhibition in bladder cancer, a genome-wide RNA-sequencing was conducted to compare gene expression profiles of UM-UC-3 cells with NONO knockdown and control.

2020-03-21 | GSE147323 | GEO

NONO Inhibits Lymphatic Metastasis of Bladder Cancer via Alternative Splicing of SETMAR.

Project description:Bladder cancer patients with lymph node (LN) metastasis have an extremely poor prognosis and no effective treatment. The alternative splicing of precursor (pre-)mRNA participates in the progression of various tumors. However, the precise mechanisms of splicing factors and cancer-related variants in LN metastasis of bladder cancer remain largely unknown. The present study identified a splicing factor, non-POU domain-containing octamer-binding protein (NONO), that was significantly downregulated in bladder cancer tissues and correlated with LN metastasis status, tumor stage, and prognosis. Functionally, NONO markedly inhibited bladder cancer cell migration and invasion in vitro and LN metastasis in vivo. Mechanistically, NONO regulated the exon skipping of SETMAR by binding to its motif, mainly through the RRM2 domain. NONO directly interacted with splicing factor proline/glutamine rich (SFPQ) to regulate the splicing of SETMAR, and it induced metastasis suppression of bladder cancer cells. SETMAR-L overexpression significantly reversed the metastasis of NONO-knockdown bladder cancer cells, both in vitro and in vivo. The further analysis revealed that NONO-mediated SETMAR-L can induce H3K27me3 at the promotor of metastatic oncogenes and inhibit their transcription, ultimately resulting in metastasis suppression. Therefore, the present findings uncover the molecular mechanism of lymphatic metastasis in bladder cancer, which may provide novel clinical markers and therapeutic strategies for LN-metastatic bladder cancer.

| S-EPMC7791011 | biostudies-literature

SETMAR regulates gene expression and alternative splicing

Project description:Transcriptomic profiling of WT and SETMAR KO HEK293T cells.

2022-08-08 | GSE181978 | GEO

CircNCOR1 suppresses lymphatic metastasis in bladder cancer

Project description:CircNCOR1 suppresses lymphatic metastasis in bladder cancer

| PRJNA789492 | ENA

S-SETMAR in the biogenesis of glioblastoma : a protective role ?

Project description:Born 45 million years ago, SETMAR is a fusion gene only present in higher primates. It is made of three exons, the two first given by the SET gene and coding for methyltransferase functions, the third given by the Hsmar1 transposase gene and coding for recombinase functions. The full length SETMAR protein (FL-SETMAR) is described as a genome keeper, expressed in main tissues, but with different levels. In cancer cells, the SETMAR gene is over-expressed, and FL-SETMAR sustains oncogenic processes, probably through its involvement in DNA repair by Non-Homologous End-Joining (NHEJ), replication stress response and chromosome decatenation. Under certain circumstances, SETMAR pre-mRNA undergoes alternative splicing, leading to the production of shorter proteins, enriched in cancer stem cells. One of them, S-SETMAR, was first discovered in glioblastoma (GB), and more recently in colorectal cancers. S-SETMAR lacks a part of the pre-SET domain and the whole SET domain, both encoded by exon 2. As a result, S-SETMAR is unable to methylate proteins, as does FL-SETMAR with a moderate efficiency. Little is known about the role of S-SETMAR. It has been recently shown that S-SETMAR, when enriched in tissues surrounding GB, correlates with an increased patient’s survival. In order to understand how S-SETMAR can have a protective role in glioblastoma biogenesis, the transcriptomes of established glioblastoma cell line expressing or not S-SETMAR were compared. This allowed the identification of deregulate pathways.

2025-10-10 | GSE255745 | GEO

SETMAR methyl-lysine (3xMBT) pull-down

Project description:SILAC labeled HT-1080 cell lysate (K0R0 and K8R10) were treated with active or catalytic inactive SETMAR methyltransferase enzyme. Samples were combined and proteins modified by methyl-lysine enriched by 3xMBT. Quantitative comparison identified candidate proteins with increase methylation following incubation with SETMAR.

2016-06-24 | PXD001635 | Pride

exosomal ELNAT1 promotes lymphatic metastasis of bladder cancer

Project description:exosomal ELNAT1 promotes lymphatic metastasis of bladder cancer

| PRJNA657414 | ENA

SETMAR regulates gene expression and alternative splicing

Project description:SETMAR regulates gene expression and alternative splicing

| PRJNA754125 | ENA

Genome-wide mapping of SETMAR transposase binding sites in the human genome

Project description:SETMAR/Metnase is a naturally occurring fusion protein that consists of a histone-lysine methyltransferase domain and an HsMar1 transposase. To elucidate the biological role of SETMAR, it is crucial to identify genomic targets to which SETMAR specifically binds and link these sites to the regulation of gene expression. Herein, we mapped the genomic landscape of SETMAR in a near-haploid human leukemia cell line (HAP1) in order to identify on-target and off-target binding sites at high resolution and to elucidate their role in terms of gene expression. Our analysis revealed a perfect correlation between SETMAR and inverted tandem repeats (ITRs) of HsMar1 transposon remnants, which are considered as natural target sites for SETMAR chromosome binding. However, we did not detect any untargeted events at non-ITR sequences, calling into question previously proposed off-target binding sites. We identified sequence fidelity of the ITR motif as a key factor for determining the binding affinity of SETMAR for chromosomes, as higher ITR fidelity resulted in increased affinity for chromatin and stronger repression of SETMAR-bound gene loci. These associations highlight how SETMAR’s chromatin binding fine-tune gene regulatory networks in human tumour cells.

2021-07-14 | GSE175725 | GEO

NONO mutations cause syndromic intellectual disability and inhibitory synaptic defects

Project description:Identifying causes of sporadic intellectual disability remains a considerable medical challenge. Here, we demonstrate that null mutations in the NONO gene, a member of the Drosophila Behavior Human Splicing (DBHS) protein family, are a novel cause of X-linked syndromic intellectual disability. Comparing humans to Nono-deficient mice revealed related behavioral and craniofacial anomalies, as well as global transcriptional dysregulation. Nono-deficient mice also showed deregulation of a large number of synaptic transcripts, causing a disorganization of inhibitory synapses, with impaired postsynaptic scaffolding of gephyrin. Alteration of gephyrin clustering could be rescued by over-expression of Gabra2 in NONO-compromised neurons. These findings link NONO to intellectual disability and first highlight the key role of DBHS proteins in functional organization of GABAergic synapses.

2015-09-02 | E-MTAB-2895 | biostudies-arrayexpress

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