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METTL3 Knockout Accelerates Hepatocarcinogenesis via Inhibiting Endoplasmic Reticulum Stress Response

ABSTRACT: METTL3 Knockout Accelerates Hepatocarcinogenesis via Inhibiting Endoplasmic Reticulum Stress Response

PROVIDER: PRJNA1222413 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32311809_1.fastq.gz	Fastqsanger.gz
	SRR32311809_2.fastq.gz	Fastqsanger.gz
	SRR32311810_1.fastq.gz	Fastqsanger.gz
	SRR32311810_2.fastq.gz	Fastqsanger.gz
	SRR32311811_1.fastq.gz	Fastqsanger.gz

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METTL3 Knockout Accelerates Hepatocarcinogenesis via Inhibiting Endoplasmic Reticulum Stress Response

Project description:Hepatocellular carcinoma (HCC) is among the most common cause of cancer-related death worldwide. Previous studies showed that N6-methyladenosine (m⁶A), the most abundant chemical modification in eukaryotic RNAs, is implicated in HCC progression. Using liver-specific conditional knockout mice, here we found that loss of METTL3, the core catalytic subunit of m⁶A methyltransferase, significantly promoted hepatic tumor initiation under various oncogenic challenges, contrary to the previously reported oncogenic role of METTL3 in liver cancer cell lines or xenograft models. Mechanistically, METTL3 deficiency accelerates HCC initiation by inhibiting m6A/Manf/endoplasmic reticulum (ER) stress response. Our findings suggest a tumor-suppressive role for METTL3 in the early stages of HCC, emphasizing the importance of understanding the dynamic role of epigenetic regulation in tumorigenesis and targeted therapy.

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Project description:In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae, and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible.

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