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Hnrnpk orchestrates embryonic growth plate development via regulating glycolysis

ABSTRACT: Hnrnpk orchestrates embryonic growth plate development via regulating glycolysis

PROVIDER: PRJNA809664 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18112733.fastq.gz	Fastqsanger.gz
	SRR18112734.fastq.gz	Fastqsanger.gz
	SRR18112735.fastq.gz	Fastqsanger.gz
	SRR18112736.fastq.gz	Fastqsanger.gz
	SRR18112737.fastq.gz	Fastqsanger.gz

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Hnrnpk orchestrates embryonic growth plate development via regulating glycolysis

Project description:Here we show a multifunctional protein, Hnrnpk, is essential for preventing excessive apoptosis and premature differentiation of growth plate chondrocytes. These datas were the RNA-seq of E18.5 growth plate chondrocytes with or without Hnrnpk.

2022-09-28 | GSE197283 | GEO

Hnrnpk maintains chondrocytes survival and function during growth plate development via regulating Hif1α-glycolysis axis.

Project description:The harmonious functioning of growth plate chondrocytes is crucial for skeletogenesis. These cells rely on an appropriate intensity of glycolysis to maintain survival and function in an avascular environment, but the underlying mechanism is poorly understood. Here we show that Hnrnpk orchestrates growth plate development by maintaining the appropriate intensity of glycolysis in chondrocytes. Ablating Hnrnpk causes the occurrence of dwarfism, exhibiting damaged survival and premature differentiation of growth plate chondrocytes. Furthermore, Hnrnpk deficiency results in enhanced transdifferentiation of hypertrophic chondrocytes and increased bone mass. In terms of mechanism, Hnrnpk binds to Hif1a mRNA and promotes its degradation. Deleting Hnrnpk upregulates the expression of Hif1α, leading to the increased expression of downstream glycolytic enzymes and then exorbitant glycolysis. Our study establishes an essential role of Hnrnpk in orchestrating the survival and differentiation of chondrocytes, regulating the Hif1α-glycolysis axis through a post-transcriptional mechanism during growth plate development.

| S-EPMC9489716 | biostudies-literature

hnRNPK knock down in Ewing cell line

Project description:Ewing sarcoma is a highly aggressive tumor characterized by a translocation between members of the FET family of RNA binding proteins and one of several ETS transcription factors, with the most common translocation being EWS-FLI1. EWS-FLI1 leads to changes in gene expression through mechanisms that are not completely understood. We performed RNA sequencing analysis on primary pediatric human mesenchymal progenitor cells (pMPCs) expressing EWS-FLI1 in order to identify novel target genes. This analysis identified lnc277 as a previously uncharacterized long non-coding RNA upregulated by EWS-FLI1 in pMPCs. Inhibiting the expression of lnc277 diminished the ability of Ewing sarcoma cell lines to proliferate and form colonies in soft agar whereas inhibiting lnc277 had no effect on other cell types tested. By analyzing gene expression after shRNA knockdown, we found that both EWS-FLI1 and lnc277 repressed many more genes that they induced and that a significant fraction of EWS-FLI1 repressed targets were also repressed by lnc277. Analysis of primary human Ewing sarcoma RNA sequencing data further supports a role for lnc277 in mediating gene repression. We identified hnRNPK as an RNA binding protein that interacts directly with lnc277. We found a significant overlap in the genes repressed by hnRNPK and those repressed by both EWS-FLI1 and lnc277, suggesting that hnRNPK participates in lnc277 mediated gene repression. Thus, lnc277 is a previously uncharacterized long non-coding RNA downstream of EWS-FLI1 that facilitates the development of Ewing sarcoma via the repression of target genes. Our studies identify a novel mechanism of oncogenesis downstream of a chromosomal translocation and underscore the importance of lncRNA-mediated gene repression as a mechanism of EWS-FLI1 transcriptional regulation. A673 Ewing cells expressing an shRNA targeting hnRNPK or control were subjected to paired end RNA sequencing and compared to shGFP control.

2014-11-01 | E-GEOD-60890 | biostudies-arrayexpress

Effect of overexpressing HNRNPK in glioblastoma stem cell

Project description:The mechanisms underlys GBM cellular transitions remain unclear.In our study, we overexpressed HNRNPK in three different types of GSCs. HNRNPK (WT) leads to high expression of core markers in GSCs, and its characteristics are similar to those of the MES subtype, exhibiting stronger invasive abilities and tumorigenic potential. We mutated 422 site from lysine(K) to argnine(R) to study the function of SUMOylation in HNRNPK. Sequencing of GSCs with overexpression of HNRNPK (K422R) mutation confirmed the upregulation of infiltrating markers within the GSCs. The changes in GSC subtypes driven by overexpression of HNRNPK (WT or K422R) were not restricted by GSC mutation features.

2024-12-13 | GSE262681 | GEO

The G Protein-Coupled Receptor ADGRG6 Maintains Mouse Growth Plate Homeostasis by Negatively Regulating IHH Signaling

Project description:ADGRG6 is a cartilage-enriched G protein-coupled receptor (GPCR). Using molecular mouse genetics and spatial transcriptomics approaches, we demonstrated that Adgrg6 has a vital role in regulating chondrocyte differentiation and growth plate homeostasis by positively regulating the formation and/or maintenance of the PTHrP (+) cell population and negatively regulating the IHH signaling in postnatal growth plates.

2024-09-19 | GSE275252 | GEO

The RNA Binding Protein HNRNPK induces p53-dependent nucleolar stress driving ribosompathy

Project description:The nucleolus is the membraneless organelle in the nucleus mainly responsible for ribosome biogenesis. It is also an excellent stress sensor and any changes on its architecture or composition leads to nucleolar stress deriving in cell cycle arrest and interruption of ribosomal activity. However, nucleolar stress sustained is also a contributing factor to pathologies like aging and cancer, highlighting the importance of its homeostasis in the cells. In this study, we identified and described the pivotal role of the RNA-binding protein Hnrnpk in the ribosome biogenesis and nucleolar dynamics. We developed an in vitro model of Hnrnpk overexpression with CRISPR-Cas9/SAM and an in vivo mouse model of Hnrnpk ubiquitous overexpression. We found that this overexpression disrupted translation and caused alterations in the nucleolar structure, resulting in nucleolar stress with alterations in the levels and localization of the nucleolar components fibrillarin and nucleolin, as well as impaired ribosome biogenesis. These aberrations trigger cell cycle arrest and cell senescence, and the phenotype could be rescued with haploinsufficiency of p53, suggesting that it is a consequence of a p53-dependant nucleolar stress mechanism. Finally, in our mouse model, Hnrnpk overexpression led to an aging phenotype with bone marrow failure and reduced lifespan, similar to a ribosomopathy-like phenotype. Together, our findings identify Hnrnpk as a novel master regulator of ribosome biogenesis and nucleolar homeostasis through p53, providing a new view of the orchestration of nucleolar integrity, ribosome function and cellular senescence.

2025-06-04 | PXD046699 | Pride

Next Generation Sequencing Analysis of control and hnRNPK-/- RKO cells Transcriptomes

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

2018-10-26 | GSE85522 | GEO

Next Generation Sequencing Analysis of Wild Type and hnRNPK-MKO liver transcription

Project description:we report liver fibrosis defects in hnRNPK Alb-Cre mice, in which hnRNPK is ablated in hepatocyte cells.

2024-06-10 | GSE176594 | GEO

hnRNPK is involved in mRNA processing of a significant fraction of the transcriptome

Project description:Here, we report the first genomic-scale comprehensive characterization of mouse transcripts bound to hnRNPK. hnRNPK binding at the isoform level was evaluated via RNA-sequencing of liver samples obtained from obese and wild-type mouse models. The comparison of hnRNPK co-immunoprecipitated fractions with total RNA fractions in a given mouse model enabled quantitative evaluation of the binding affinity of hnRNPK for thousands of isoforms.

2015-10-01 | GSE65887 | GEO

RNA binding of CBFB and hnRNPK

Project description:RNA immunoprecipitation assay followed by next generation sequencing (RIPseq) to identify RNAs bound by CBFB and hnRNPK in breast cells.

2019-04-18 | GSE119800 | GEO

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