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NFE2L3 Drives Hepatocellular Carcinoma Proliferation via Regulating the Proteasome-Dependent Degradation of ISGylation p53 through interaction with TRIM25.

ABSTRACT: NFE2L3 Drives Hepatocellular Carcinoma Proliferation via Regulating the Proteasome-Dependent Degradation of ISGylation p53 through interaction with TRIM25.

PROVIDER: PRJNA867580 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR20983603_1.fastq.gz	Fastqsanger.gz
	SRR20983603_2.fastq.gz	Fastqsanger.gz
	SRR20983604_1.fastq.gz	Fastqsanger.gz
	SRR20983604_2.fastq.gz	Fastqsanger.gz
	SRR20983605_1.fastq.gz	Fastqsanger.gz

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NFE2L3 Drives Hepatocellular Carcinoma Proliferation via Regulating the Proteasome-Dependent Degradation of ISGylation p53 through interaction with TRIM25.

Project description:To investigate the function of NFE2L3 and NFE2L3△C(557-694aa) in the regulation of hepatocellular carcinoma proliferation, we established HepG2 cell lines in which the target gene has been over express by lentiviruses. We then performed gene expression profiling analysis using data obtained from RNA-seq of 3 different cells at three-time points.

2023-09-13 | GSE210803 | GEO

NFE2L3 drives hepatocellular carcinoma cell proliferation by regulating the proteasome-dependent degradation of ISGylated p53.

Project description:Nuclear factor erythroid 2-like 3 (NFE2L3) is a member of the cap 'n' collar basic-region leucine zipper (CNC-bZIP) transcription factor family that plays a vital role in modulating oxidation-reduction steady-state and proteolysis. Accumulating evidence suggests that NFE2L3 participates in cancer development; however, little is known about the mechanism by which NFE2L3 regulates hepatocellular carcinoma (HCC) cell growth. Here, we confirmed that NFE2L3 promotes HCC cell proliferation by acting as a transcription factor, which directly induces the expression of proteasome and interferon-stimulated gene 15 (ISG15) to enhance the proteasome-dependent degradation of ISGylated p53. Post-translational ISGylation abated the stability of p53 and facilitated HCC cell growth. In summary, we uncovered the pivotal role of NFE2L3 in promoting HCC cell proliferation during proteostasis. This finding may provide a new target for the clinical treatment of HCC.

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TRIM25

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Nfe2l3 promotes neuroprotection and long-distance axon regeneration after injury in vivo [bulkRNA-seq]

Project description:Nuclear factor erythroid 2 like (Nfe2l) gene family members 1-3 mediate cellular response to oxidative stress, including in the central nervous system (CNS). However, neuronal functions of Nfe2l3 are unknown. Here, we comparatively evaluated expression of Nfe2l1, Nfe2l2, and Nfe2l3 in singe cell RNA-seq (scRNA-seq)-profiled cortical and retinal ganglion cell (RGC) CNS projection neurons, investigated whether Nfe2l3 regulates neuroprotection and axon regeneration after CNS injury in vivo, and characterized a gene network associated with Nfe2l3 in neurons. We showed that, Nfe2l3 expression transiently peaks in developing immature cortical and RGC projection neurons, but is nearly abolished in adult neurons and is not upregulated after injury. Furthermore, within the retina, Nfe2l3 is enriched in RGCs, whereas Nfe2l1 and Nfe2l2 are expressed robustly in other retinal cell types as well, and are also upregulated after injury. We also found that, expressing Nfe2l3 in injured RGCs through localized intralocular viral vector delivery promotes neuroprotection and long-distance axon regeneration after optic nerve injury in vivo. Moreover, Nfe2l3 treatment provided a similar extent of neuroprotection and axon regeneration as viral vector-targeting of Pten and Klf9, which are prominent regulators of neuroprotection and long-distance axon regeneration. Finally, we bioinformatically characterized a gene network associated with Nfe2l3 in neurons, which revealed the association of Nfe2l3 with established mechanisms of neuroprotection and axon regeneration. Thus, Nfe2l3 is a novel neuroprotection and axon regeneration-promoting factor with a therapeutic potential for treating CNS injury and disease.

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Nfe2l3 promotes neuroprotection and long-distance axon regeneration after injury in vivo [Third party: scRNA-seq]

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Exogenous RNA surveillance by proton-sensing TRIM25

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Project description:In order to determine how NAT10 regulates NFE2L3 to promote the progression of ccRCC, since NFE2L3 is a transcription factor, we performed CHP-seq detection for NFE2L3, as well as RNA-seq detection for 786-O cells with stable NFE2L3 knocking and control 786-O cells. The results of RNA-seq showed that 312 transcripts in the NFE2L3 knockdown group were down-regulated, and 3 114 transcripts in the previous ccRCC tissue were up-regulated. Moreover, after comprehensive analysis of ChIP-seq, there were 12 overlapping transcripts. Analysis of the expression levels of 12 transcripts in control cells and stable NFE2L3 knockout cells showed that the expression level of LASP1 was the highest in cells, so we hypothesized that NFE2L3 promoted the progression of ccRCC by affecting LASP1.

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NAT10 promotes the progression of clear cell renal cell carcinoma by regulating ac4C acetylation of NFE2L3 and activating AKT/GSK3β signaling pathway [ChIP-seq]

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RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination

Project description:TRIM25 E3 ubiquitin ligase is a new RNA-binding protein. We present the first high-throughput analysis of the molecular interactomes of TRIM25. We show that TRIM25 is a bona fide RNA-binding protein that interacts with numerous coding and non-coding transcripts. This suggests that TRIM25 could play a role in the regulation of RNA metabolism.

2018-07-27 | GSE104949 | GEO

The molecular dissection of TRIM25‘s RNA-binding mechanism provides key insights into its antiviral activity

Project description:TRIM25 is an RNA-binding ubiquitin E3 ligase with central but poorly understood roles in the innate immune response to RNA viruses. The link between TRIM25’s RNA binding and its role in innate immunity has not been established. Thus, we utilized a multitude of biophysical techniques to identify key RNA-binding residues of TRIM25 and developed an RNA-binding deficient mutant (TRIM25-m9). Using iCLIP2 in virus-infected and uninfected cells, we identified TRIM25’s RNA sequence and structure specificity, that it binds specifically to viral RNA, and that the interaction with RNA is critical for its antiviral activity.

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