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Translatome profiling of warm temperature (35°C -> 38.5°C) treated mouse embryonic fibroblast cells in the presense or absence of PI3K inhibitor, 17β-hydroxy wortmannin

ABSTRACT: Translatome profiling of warm temperature (35°C -> 38.5°C) treated mouse embryonic fibroblast cells in the presense or absence of PI3K inhibitor, 17β-hydroxy wortmannin

PROVIDER: PRJNA870739 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR21119900.fastq.gz	Fastqsanger.gz
	SRR21119897.fastq.gz	Fastqsanger.gz
	SRR21119898.fastq.gz	Fastqsanger.gz
	SRR21119899.fastq.gz	Fastqsanger.gz

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Translatome profiling of warm temperature (35°C -> 38.5°C) treated mouse embryonic fibroblast cells in the presense or absence of PI3K inhibitor, 17β-hydroxy wortmannin

Project description:To see a possible effect of PI3K inhibition on a physiological warm temperature shift (WTS, 35°C to 38.5°C)-induced ribosomal accumulation on the Per2 minimal uORF, we performed Ribo-seq using dexamethasone-synchronized WTS-treated mouse embryonic fibroblast cells with or without 17β-hydroxy wortmannin (wortm) treatment at a circadain rising phase of Per2.

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Transcriptome and translatome profiling of warm temperature (35°C -> 38.5°C) treated mouse embryonic fibroblast cells

Project description:Transcriptome and translatome profiling of warm temperature (35°C -> 38.5°C) treated mouse embryonic fibroblast cells

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Project description:17β-hydroxysteroid dehydrogenase-13 (17β-HSD13) is a liver-rich lipid droplet associated protein, encoding by gene HSD17B13, that acted as an important regulator of hepatic lipid metabolism. Increased expression of 17β-HSD13 promotes hepatic lipid accumulation in rodents, and a common loss-of-function variant of HSD17B13 (rs72613567: TA) is related to better outcome in patients with various chronic liver diseases. To understand the role of 17β-HSD13 in liver lipid metabolism under normal and high-fat feeding conditions, we characterized the effect of protein phosphorylation of 17β-HSD13 on hepatic lipid homeostasis. We identify Ser33 as an important protein kinase A (PKA)-mediated phosphorylation site of 17β-HSD13 that physically interact with ATGL and facilitates its translocation to lipid droplets to enhance lipolysis. Mutation of Ser33 to Ala (S33A) in 17β-HSD13 reduces ATGL-dependent lipolysis and increases lipid droplet size in cultured hepatocytes by reducing CGI-58-mediated ATGL activation. Consistently, a transgenic knock-in mouse strain carrying HSD17B13 S33A mutation (HSD17B1333A/A) spontaneously develops liver steatosis with reduced lipolysis. Moreover, HSD17B1333A/A mice are more prone to high fat-induced hepatic steatosis and inflammation. Finally, we found Reproterol, a potential HSD17B13 modulator and FDA-approved drug, confers a protection against liver steatosis possibly through phosphorylation of 17β-HSD13 at Ser33 in a PKA-dependent manner. In summary, we demonstrate a critical role and the underlying mechanism of hepatic 17β-HSD13 phosphorylation in the pathogenesis of NAFLD. Our findings highlight the potential of targeting 17β-HSD13 phosphorylation as a novel therapeutic approach for NAFLD.

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