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E3 ligase SYVN1-Mediated Polyubiquitination of CPSF6 Promotes Alternative Polyadenylation and Antivirus Effects of Macrophages

ABSTRACT: E3 ligase SYVN1-Mediated Polyubiquitination of CPSF6 Promotes Alternative Polyadenylation and Antivirus Effects of Macrophages

PROVIDER: PRJNA1199446 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31752725_1.fastq.gz	Fastqsanger.gz
	SRR31752725_2.fastq.gz	Fastqsanger.gz
	SRR31752726_1.fastq.gz	Fastqsanger.gz
	SRR31752726_2.fastq.gz	Fastqsanger.gz
	SRR31752727_1.fastq.gz	Fastqsanger.gz

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E3 ligase SYVN1-Mediated Polyubiquitination of CPSF6 Promotes Alternative Polyadenylation and Antivirus Effects of Macrophages

Project description:Down-regulation of CPSF6 protein, one of 3′ end processing factors, mediates APA in macrophage with responses to virus infection and plays an important role in its anti-virus effect. However, the signal pathway and molecular mechanism underlying the downregulation of the CPSF6 protein remain elusive. Here, we found that MAVS triggers the nucleus import of E3 ligase SYVN1 mediated by NUP153 in response to vesicular stomatitis virus infection. Then, SYVN1 catalyzes K48-linked polyubiquitination of CPSF6, resulting in the degradation of CPSF6 via proteasome, and then transcriptome wide APA and anti-virus effect subsequently.

2024-12-21 | GSE284508 | GEO

Phosphorylation of CPSF6 RS-like domain

Project description:Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor CPSF6, regulates alternative polyadenylation (APA). CPSF6 has a RS-like domain which plays role in protein -protein interactions. This interaction might have role in alternative polyadenylation site selection. The phosphorylation of RS- like domain might play role in protein -protein interaction and thus might have a role in alternative polyadenylation site selection. So we did mass specteroanalysis to analyse phosphorylation sites of RS-like domain of CPSF6.

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E3 ligase TRIP12 affecting EZH2 ubiquitination in ENKTL

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EGFR is a target of the tumor suppressor E3-ligase FBXW7

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The Hace1 E3 Ligase Modulates the Activity of Multiple Tumor Suppressive CRL E3 Ligases by binding to CAND1

Project description:The Hace1 E3 ligase is a tumor suppressor in stressed cells. Through unknown mechanisms, Hace1 indirectly targets the cyclin D1 proto-oncogene for proteasomal degradation during nutrient depletion. We now show that Hace1 targets HIF1alpha for VHL-dependent degradation during hypoxia. To better understand these diverse actions we performed mass spectrometry to identify Hace1-interacting proteins. We show that Hace1 interacts with cullin-associated NEDD8-dissociated protein 1 (CAND1) under nutrient depletion and hypoxia. CAND1 binds cullins and prevents their entry into cullin ring E3 ligase (CRL) complexes, thus blocking CRL activity. Hace1 binding releases CUL1/2 from CAND1, facilitating assembly of CRL complexes to degrade cyclin D1 and HIF1alpha, respectively. These findings suggest a broad role for Hace1 in regulating tumor suppressive CRL E3 ligases. In this study, we used gene expression profiling to characterize how Hace1 overexpression affect the transcriptional response to hypoxic stress Using Affymetrix exon-level microarrays, we compared the expression profile of HEK293 cells overexpressing either Hace1 or MSCV vector alone, under hypoxia or normoxia

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Project description:The hypoxia-inducible factor 1-α (HIF-1α) enables cells to adapt and respond to hypoxia (Hx), and the activity of this transcription factor is regulated by several oncogenic signals and cellular stressors. While the pathways controlling normoxic degradation of HIF-1α are well understood, the mechanisms supporting the sustained stabilization and activity of HIF-1α under Hx are less clear. We report that ABL kinase activity protects HIF-1α from proteasomal degradation during Hx. Using a fluorescence-activated cell-sorting (FACS)-based CRISPR/Cas9 screen, we identified HIF-1α as a substrate of the cleavage and polyadenylation specificity factor-1 (CPSF1), an E3-ligase which targets HIF-1α for degradation in the presence of an ABL kinase inhibitor in Hx.

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E3 ubiquitin ligase DTX2 reinforces innate antiviral immune responses by modulating K63-linked ubiquitination of TBK1

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BRCT phosphoprotein recognition, but not E3 ligase activity, is essential for BRCA1 tumor suppression

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