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Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [si-oligo vs si-PTBP1]

ABSTRACT: Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [si-oligo vs si-PTBP1]

PROVIDER: PRJNA714554 | ENA |

REPOSITORIES: ENA

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Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [si-oligo vs si-PTBP1]

Project description:Function exploration of hsa_circ_0005358 in cervical cancer cells ;Mechanism of how hsa_circ_0005358 works via its protein partner PTBP1.

2022-06-14 | GSE168907 | GEO

Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA

Project description:Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA

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Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [vector vs has_circ005358 overexpression]

Project description:Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [vector vs has_circ005358 overexpression]

| PRJNA708268 | ENA

Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA [vector vs has_circ005358 overexpression]

Project description:Functional exploration of hsa_circ_0005358 in cervical cancer cells ;Mechanism of how hsa_circ_0005358 works via its protein partner PTBP1.

2022-06-14 | GSE168549 | GEO

hsa_circ_0005358 suppresses cervical cancer metastasis by interacting with PTBP1 protein to destabilize CDCP1 mRNA.

Project description:Metastasis is the main cause of cervical cancer lethality, but to date, no effective treatment has been developed to block metastasis. Circular RNAs (circRNAs) were recently found to be involved in cancer metastasis. In this study, we identified a downregulated circRNA derived from the host gene Gli1 (hsa_circ_0005358) in cervical cancer tissues, which was expressed at lower levels in tissues with extracervical metastasis than in those without extracervical metastasis. Upregulation of hsa_circ_0005358 significantly suppressed the migration and invasion of cervical cancer cells in vitro, and downregulation of hsa_circ_0005358 had the opposite effect. A mouse model revealed that cervical cancer cells overexpressing hsa_circ_0005358 possessed weaker metastatic potential in vivo. RNA-pull-down assay, mass spectrometry, and RNA immunoprecipitation validated the findings that hsa_circ_0005358 functions via its 215-224 sequence, which interacts with polypyrimidine tract-binding protein 1 (PTBP1). RNA-sequencing profiling revealed that CUB-domain-containing protein 1 (CDCP1) is a common target for hsa_circ_0005358 and PTBP1. We further confirmed that hsa_circ_0005358 sequestered PTBP1, preventing it from stabilizing CDCP1 mRNA, reducing CDCP1 protein translation and ultimately suppressing cancer metastasis. Our findings reveal the function of hsa_circ_0005358 in tumor metastasis, which may be applied to a potential therapeutic approach for patients with metastatic cervical cancer.

| S-EPMC8693350 | biostudies-literature

iiCLIP protocol benchmarking with PTBP1

Project description:We describe an improved individual nucleotide resolution CLIP protocol (iiCLIP), which can be completed within 4 days from UV crosslinking to libraries for sequencing. For benchmarking, we directly compared PTBP1 iiCLIP libraries with the iCLIP2 protocol produced under standardised conditions with 1 million HEK293 cells, and with public eCLIP and iCLIP PTBP1 data. There are 3 PTBP1 iiCLIP libraries, 1 input iiCLIP library and 1 PTBP1 iCLIP2 library produced in this study.

2022-08-01 | E-MTAB-10881 | biostudies-arrayexpress

Proteome changes in PTBP1 deficient hematopoietic cells

Project description:Ribosomopathies constitute a range of disabling conditions associated with defective protein synthesis mainly affecting hematopoietic stem cells (HSCs) and erythroid development. Here we demonstrate that deletion of Polypyrimidine Tract Binding Protein 1 (PTBP1) in the hematopoietic compartment led to the development of a ribosomopathy-like condition. Specifically, loss of PTBP1 was associated with a decrease in HSC self-renewal, erythroid differentiation and protein synthesis. Consistent with its function as a splicing regulator, PTBP1 deficiency led to splicing defects in hundreds of genes and we demonstrate that the up-regulation of a specific isoform of CDC42 could partly mimic the protein synthesis defect associated with loss of PTBP1. Furthermore, PTBP1 deficiency was associated with a marked defect in ribosome biogenesis and a selective reduction in the translation of mRNAs encoding ribosomal proteins. Collectively, this work identifies PTBP1 as a key integrator of ribosomal functions and highlights the broad functional repertoire of RNA binding proteins.

2022-05-04 | PXD023879 | Pride

PTBP1 - Modified iCLIP

Project description:PTBP1 - Modified iCLIP

| PRJEB15236 | ENA

Hsa_circ_0005358 suppresses cervical cancer metastasis via interacting with PTBP1 protein to destabilize CDCP1 mRNA

Project description:This SuperSeries is composed of the SubSeries listed below.

2022-06-14 | GSE168909 | GEO

Next Generation Sequencing of si-NC and si-circFAM120A Transcriptomes

Project description:Purpose: to find the potential down-stream target gene of circFAM120A Methods: mRNA profiles of decidualized human endometrial stromal cells (hESCs) after down-regulated FAM120A and control using siRNA were generated by NGS and compared by bioinformatics analysis Results: we sequenced 26414 mRNAs in hESCs between the si-NC and si-circFAM120A groups and identified 242 differentially expressed mRNAs, between which 161 were downregulated and 81 were up-regulated in si-circFAM120A group Conclusions: Our study represents the detailed analysis of decidualized hESCs transcriptomes between si-NC and si-circFAM120A groups.

2023-06-30 | GSE174495 | GEO

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