Oct 30, 2018

The proteasome biogenesis regulator Rpn4 cooperates with the unfolded protein response to promote resistance to endoplasmic reticulum stress

BioRxiv : the Preprint Server for Biology
Rolf M Schmidt, Sebastian Schuck

Abstract

Misfolded proteins in the endoplasmic reticulum (ER) activate the unfolded protein response (UPR), which enhances protein folding to restore homeostasis. Additional pathways respond to ER stress, but how they help counteract protein misfolding is incompletely understood. Here, we develop a titratable system for the induction of ER stress in yeast to enable a genetic screen for factors that augment stress resistance independently of the UPR. We identify the proteasome biogenesis regulator Rpn4 and show that it cooperates with the UPR. Rpn4 abundance increases during ER stress, first by a post-transcriptional, then by a transcriptional mechanism. Induction of RPN4 transcription is triggered by cytosolic mislocalization of secretory proteins, is mediated by multiple signaling pathways and accelerates clearance of misfolded proteins from the cytosol. Thus, Rpn4 and the UPR are complementary elements of a modular cross-compartment response to ER stress.

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Mentioned in this Paper

Biochemical Pathway
Proteasome Pathway
RPN4
RPN4 protein, S cerevisiae
PSMD9
Response to Endoplasmic Reticulum Stress
Unfolded Protein Response
Transcription, Genetic
Genetic Screening (Procedure)
Yeasts

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