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Coordination of UPR-related gene expression in early plasma cells by mTORC1

ABSTRACT: Coordination of UPR-related gene expression in early plasma cells by mTORC1

PROVIDER: PRJNA593421 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR10584200.fastq.gz	Fastqsanger.gz
	SRR10584300.fastq.gz	Fastqsanger.gz
	SRR10584201.fastq.gz	Fastqsanger.gz
	SRR10584301.fastq.gz	Fastqsanger.gz
	SRR10584202.fastq.gz	Fastqsanger.gz

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Coordination of UPR-related gene expression in early plasma cells by mTORC1

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Project description:Although stress responses, such as the unfolded stress response (UPR), have been extensively studied upon induction by harsh stressors, endogenous functions of these protective pathways remain less well understood. We previously found that the UPR is activated during meiosis in budding yeast, and here we investigate its role. We find that endogenous UPR activation during the meiotic divisions does not lead to a broad transcriptional program as reported for drug-triggered UPR activation and is dispensable for gamete formation. In contrast, we find that the endogenous UPR activation that occurs just prior to meiosis is required for meiotic entry and thus gamete production. Only a small subset of known UPR transcriptional targets are part of this response, and the role of the pre-meiotic UPR can be replaced by increasing ER chaperone levels, reducing bulk translation, or reducing expression of the translocation factor Sec61. Together, these findings indicate that physiological meiosis-associated UPR activation supports normal proteostasis in multiple ways to prepare cells for meiotic entry, including by reducing expression of translation factors. In support of a model that ER function is compromised in pre-meiotic cells lacking the UPR, foci of reticulon proteins are present in these cells and their presence correlates with an inability of cells to enter meiosis. Overall, our study reveals surprising features of a physiological UPR activation event, including that its critical targets are minimal and that they support normal ER structure. 

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