ArticleMolecular biology of the cell2009
Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 66 citations in OpenAlex.
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- The Erv41-Erv46 complex serves as a retrograde receptor to retrieve misfolded secretory proteins that have escaped from the ER.Molecular biology of the cell · 2025Article
- Regulation of ubiquitin-proteasome system and its relative pathways in pancreatic adenocarcinoma.BioImpacts : BI · 2025Review
- Proteotoxic stress and the ubiquitin proteasome system.Seminars in cell & developmental biology · 2024Review
- MitoStores: chaperone-controlled protein granules store mitochondrial precursors in the cytosol.The EMBO journal · 2023Article
- Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress.PLoS biology · 2023Article
- Distinct classes of misfolded proteins differentially affect the growth of yeast compromised for proteasome function.FEBS letters · 2021Article
- Increased levels of mitochondrial import factor Mia40 prevent the aggregation of polyQ proteins in the cytosol.The EMBO journal · 2021Article
- Reg1 and Snf1 regulate stress-induced relocalization of protein phosphatase-1 to cytoplasmic granules.The FEBS journal · 2021Article
- Many, but not all, lineage-specific genes can be explained by homology detection failure.PLoS biology · 2020Article
- The intermembrane space protein Mix23 is a novel stress-induced mitochondrial import factor.The Journal of biological chemistry · 2020Article
- HRD Complex Self-Remodeling Enables a Novel Route of Membrane Protein Retrotranslocation.iScience · 2020Article
- Article
- Global Proteome Remodeling during ER Stress Involves Hac1-Driven Expression of Long Undecoded Transcript Isoforms.Developmental cell · 2018Article
- Protein aggregation into insoluble deposits protects from oxidative stress.Redox biology · 2017Article
- Editing of misaminoacylated tRNA controls the sensitivity of amino acid stress responses in Saccharomyces cerevisiae.Nucleic acids research · 2017Article
- Phospholipase Lpl1 links lipid droplet function with quality control protein degradation.Molecular biology of the cell · 2017Article
- Expression of three topologically distinct membrane proteins elicits unique stress response pathways in the yeast Saccharomyces cerevisiae.Physiological genomics · 2015Article
- Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Molecular biology of the cell · 2015Article
- Distinct activation of an E2 ubiquitin-conjugating enzyme by its cognate E3 ligases.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
ER quality control (ERQC) prevents the exit of misfolded secretory and membrane proteins from the ER. A critical aspect of ERQC is a transcriptional response called the unfolded protein response (UPR), which up-regulates genes that enable cells to cope with misfolded, ER-retained proteins. In this study, we compare the transcriptional responses in yeast resulting from the acute expression of misfolded proteins residing in three different cellular compartments (the ER lumen, membrane, and cytosol), and find that each elicits a distinct transcriptional response. The classical UPR response, here-designated UPR-L, is induced by the ER lumenal misfolded protein, CPY*. The UPR-Cyto response is induced by the cytosolic protein, VHL-L158P, and is characterized by a rapid, transient induction of cytosolic chaperones similar to the heat-shock response. In contrast, the misfolded membrane protein with a cystolic lesion, Ste6p*, elicits a unique response designated UPR-M/C, characterized by the modest induction of >20 genes regulated by Rpn4p, an activator of proteasomal genes. Independently, we identified several genes required for yeast viability during UPR-M/C stress, but not UPR-L or UPR-Cyto stress. Among these is RPN4, highlighting the importance of the Rpn4p-dependent response in tolerating UPR-M/C stress. Further analysis suggests the requirement for Rpn4p reflects severe impairment of the proteasome by UPR-M/C stress.
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