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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (Total RNA-Seq)

ABSTRACT: Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (Total RNA-Seq)

PROVIDER: PRJNA1163021 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30731985_1.fastq.gz	Fastqsanger.gz
	SRR30731985_2.fastq.gz	Fastqsanger.gz
	SRR30731986_1.fastq.gz	Fastqsanger.gz
	SRR30731986_2.fastq.gz	Fastqsanger.gz
	SRR30731987_1.fastq.gz	Fastqsanger.gz

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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (scRNA-Seq)

Project description:Lung metastases are detected in more than half of patients with metastatic tumors. However, it remains largely unknown why the lung environment is a permissive niche for metastases. Here, we discover that pulmonary aspartate triggers a cellular signaling cascade in disseminated cancer cells resulting in a translational program that boosts lung metastasis. Specifically, we observe that patients and mice with breast cancer have high concentrations of aspartate in their lung interstitial fluid. This extracellular aspartate activates the ionotropic N-methyl-D-aspartate (NMDA) receptor in cancer cells, which induces CREB-dependent mRNA expression of deoxyhypusine hydroxylase (DOHH). The latter is essential for hypusination, a posttranslational modification required for the activity of the non-classical translation initiation factor eIF5A. In turn, a translational program with TGF-β signaling as a central hub promotes collagen remodeling in the disseminated breast cancer cells. We detect key aspects of this mechanism in lung metastases from patients with breast cancer. In summary, we discover that pulmonary aspartate increases with breast cancer and induces a signaling cascade promoting the growth of lung metastases.

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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (Polysomal RNA-Seq)

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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation

Project description:Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation

| PRJNA988804 | ENA

Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (scRNA-Seq)

Project description:Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (scRNA-Seq)

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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (Polysomal RNA-Seq)

Project description:Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation (Polysomal RNA-Seq)

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Aspartate signaling increases the aggressiveness of lung metastases by inducing eIF5A-mediated translation

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

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Ribosome profiling study of eIF5A depletion strain

Project description:The eukaryotic translation factor eIF5A, originally identified as an initiation factor, was later shown to promote translation elongation of iterated proline sequences. Using a combination of ribosome profiling and in vitro biochemistry, we report a much broader role for eIF5A in elongation and uncover a substantial function for eIF5A in termination. Ribosome profiling of an eIF5A-depleted strain reveals a global elongation defect, with abundant ribosomes stalling at many sequences, not limited to proline stretches. Our data also show accumulation at stop codons and in the 3’-UTR, suggesting a global defect in termination in the absence of eIF5A. Using an in vitro reconstituted translation system, we find that eIF5A strongly promotes the translation of novel stalling sequences and increases the rate of peptidyl-tRNA hydrolysis more than 17-fold. We conclude that eIF5A functions broadly in elongation and termination, rationalizing its great cellular abundance and essential nature.

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Study of ribosome dynamics after eIF5A depletion in budding yeast

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