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Overexpression of CLK and wild-type CPSF6 and mutant CPSF6 in HEK293T cells to verify the effect of CLK2 phosphorylation CPSF6 on APA

ABSTRACT: Overexpression of CLK and wild-type CPSF6 and mutant CPSF6 in HEK293T cells to verify the effect of CLK2 phosphorylation CPSF6 on APA

PROVIDER: PRJNA962593 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24467467.fastq.gz	Fastqsanger.gz
	SRR24467468.fastq.gz	Fastqsanger.gz
	SRR24467469.fastq.gz	Fastqsanger.gz
	SRR24467470.fastq.gz	Fastqsanger.gz
	SRR24467471.fastq.gz	Fastqsanger.gz

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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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The transcriptome-wide CPSF6-induced APA alterations in HCC cells

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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Overexpression of CLK and wild-type CPSF6 and mutant CPSF6 in HEK293T cells to verify the effect of CLK2 phosphorylation CPSF6 on APA

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

2023-09-07 | GSE230814 | 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.

2019-04-01 | PXD012713 | Pride

The transcriptome-wide CPSF6-induced APA alterations in HCC cells

Project description:The transcriptome-wide CPSF6-induced APA alterations in HCC cells

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

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

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CPSF6 regulates alternative polyadenylation and proliferation of cancer cell through phase separation

Project description:In order to explore the impact of phase separation of CPSF6 on APA, we identified the structural domains that affect its phase separation formation and performed mutations. In addition, we also found that the phosphorylation of CPSF6 can also affect its phase separation effect, and identified key kinases. We performed IVT-SAPAS sequencing on both cases mentioned above.

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Proteins that interact with CLK2 (WT) or CLK2 (T343A)

Project description:Our results show that CLK2 undergoes liquid-liquid phase separation (LLPS) in response to heat shock stress. Phosphorylation of CLK2 at T343 prevents the LLPS of CLK2. To identify the proteins that recruited to the CLK2 condensates, we immunoprecipitated CLK2 (WT) or (T343A) proteins with FLAG antibody and performed mass spectrometry to detect the interacting proteins.

2023-11-06 | PXD040997 | Pride

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