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The transcriptome-wide CPSF6-induced APA alterations in gastric cancer cells

ABSTRACT: The transcriptome-wide CPSF6-induced APA alterations in gastric cancer cells

PROVIDER: PRJEB42340 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	ERR5043170_1.fastq.gz	Fastqsanger.gz
	ERR5043170_2.fastq.gz	Fastqsanger.gz
	ERR5043171_1.fastq.gz	Fastqsanger.gz
	ERR5043171_2.fastq.gz	Fastqsanger.gz
	ERR5043172_1.fastq.gz	Fastqsanger.gz

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The transcriptome-wide CPSF6-induced APA alterations in gastric cancer cells

Project description:In this study, we showed that knockdown of CPSF6 inhibited GC cell growth and promoted apoptosis in vitro and in vivo. In order to understand the underlying mechanisms of CPSF6, we performed an APA profiling analysis in wild-type and CPSF6-knockdown AGS cells, using 3T-seq method.

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Project description:In this study, we showed that CPSF6 promoted HCC cell growth, migration and metastasis in vitro and in vivo. In order to understand the underlying mechanisms of CPSF6, we aimed to perform a APA profiling analysis in hepatocyte and hepatoma carcinoma cells under different CPSF6 expression conditions using 3T-seq method.

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CPSF role on APA regulation

Project description:We found that CPSF6, a component of the CFIm, can form liquid-liquid phase separation (LLPS) and the elevated LLPS induces the preferential usage of the distal poly(A) sites. CLK2, a kinase upregulated in cancer cells, destructs LLPS of CPSF6 by phosphorylating its arginine/serine-like domain. Albeit higher expression of CPSF6 in cancer, the reduction of LLPS leads to shortening 3’ UTR of cell cycle related genes and then promotes cell proliferation. These results reveal that LLPS regulation of CPSF6 is a fine tuning way of APA in cancer cells and provide a new mechanism for APA regulation by regulating LLPS of 3’ end processing factors through post-translational modification.

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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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CPSF6 regulates alternative polydenylation and proliferation of cancer cell through phase separation Ⅱ

Project description:To verify the effect of phosphorylation of CPSF6 by CLK2 on APA, we co overexpressed CLK2 and wild-type CPSF6 or phosphorylated mutant CPSF6 in HEK293T cells

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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.

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