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Modulation of m6A RNA Methylation by Death Associated Protein 3 (DAP3) [eCLIP-seq]

ABSTRACT: Modulation of m6A RNA Methylation by Death Associated Protein 3 (DAP3) [eCLIP-seq]

PROVIDER: PRJNA994837 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25276775_1.fastq.gz	Fastqsanger.gz
	SRR25276775_2.fastq.gz	Fastqsanger.gz
	SRR25276776_1.fastq.gz	Fastqsanger.gz
	SRR25276776_2.fastq.gz	Fastqsanger.gz
	SRR25276777_1.fastq.gz	Fastqsanger.gz

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Modulation of m6A RNA Methylation by Death Associated Protein 3 (DAP3)

Project description:Modulation of m6A RNA Methylation by Death Associated Protein 3 (DAP3)

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Suppression of adenosine-to-inosine (A-to-I) RNA editome by death associated protein 3 (DAP3) promotes cancer progression

Project description:RNA editing introduces nucleotide changes in RNA sequences. Recent studies have reported that aberrant A-to-I RNA editing profiles are implicated in cancers. Albeit changes in expression and activity of ADAR genes are thought to have been responsible for the dysregulated RNA editome in diseases, they are not always correlated, indicating the involvement of secondary regulators. Here, we uncover DAP3 as a potent repressor of editing and a strong oncogene in cancer. DAP3 mainly interacts with the deaminase domain of ADAR2 and represses editing via disrupting association of ADAR2 with its target transcripts. PDZD7, an exemplary DAP3-repressed editing target, undergoes a protein recoding editing at stop codon [Stop →Trp (W)]. Because of editing suppression by DAP3, the unedited PDZD7WT, which is more tumorigenic than edited PDZD7Stop518W, is accumulated in tumors. In sum, cancer cells may acquire malignant properties for their survival advantage through suppressing RNA editome by DAP3.

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Death Associated Protein 3 (DAP3) Coordinates Splicing Regulatory Networks to Modulate Global Alternative Splicing in Cancer

Project description:The dynamic regulation of transcriptome requires coordinated participation of multiple RNA binding proteins (RBPs) in RNA processing. Dysregulated RNA processing, such as aberrant alternative splicing, is implicated in many cancers. Therefore, it is critical to explore the cancer-related RNA processing regulation and the underlying mechanisms. Many RBPs lack classical RNA-binding domains and their functions in RNA processing regulation remain unclear. Through an unbiased transcriptome-wide analysis, we report DAP3 binds ubiquitously to endogenous RNAs in vivo and its depletion reshapes the alternative splicing landscape in cancer cells. Mechanistically, we show DAP3 coordinates splicing regulatory networks, not only via mediating the formation of ribonucleoprotein (RNP) complexes, but also via modulating splicing of numerous splicing factors. Specific DAP3-regulated splicing changes such as non-productive splicing of WSB1 and RBM6, play important roles in tumorigenesis. Together, these findings provide critical mechanistic insights into the molecular functions of DAP3 in cancer development as a master regulator of RNA processing.

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