ArticleMolecular biology of the cell2012
Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Distinct classes of misfolded proteins differentially affect the growth of yeast compromised for proteasome function.FEBS letters · 2021Article
- Endoplasmic Reticulum Subproteome Analysis Reveals Underlying Defense Mechanisms of Wheat Seedling Leaves under Salt Stress.International journal of molecular sciences · 2021Article
- Characterization of a novel nicotinamide adenine dinucleotide-cytochrome b5 reductase mutation associated with canine hereditary methemoglobinemia.The Journal of veterinary medical science · 2021Article
- Putative Interaction Proteins of the Ubiquitin Ligase Hrd1 inEvolutionary bioinformatics online · 2018Article
- Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway.The Journal of cell biology · 2015Article
- Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.Molecular biology of the cell · 2015Article
- The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Molecular biology of the cell · 2015Article
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- Misfolded proteins induce aggregation of the lectin Yos9.The Journal of biological chemistry · 2014Article
- Three old and one new: protein import into red algal-derived plastids surrounded by four membranes.Protoplasma · 2013Review
- BINDING PROTEIN is a master regulator of the endoplasmic reticulum stress sensor/transducer bZIP28 in Arabidopsis.The Plant cell · 2013Article
- A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.The Journal of biological chemistry · 2013Article
- The endoplasmic reticulum-associated degradation pathways of budding yeast.Cold Spring Harbor perspectives in biology · 2012Review
- Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Critical reviews in biochemistry and molecular biologyReview
- Enhancing Yeast Surface Display: UPR, ERAD, and ER Dynamics in Recombinant Protein Production.Food technology and biotechnologyReview
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER) has an elaborate quality control system, which retains misfolded proteins and targets them to ER-associated protein degradation (ERAD). To analyze sorting between ER retention and ER exit to the secretory pathway, we constructed fusion proteins containing both folded carboxypeptidase Y (CPY) and misfolded mutant CPY (CPY*) units. Although the luminal Hsp70 chaperone BiP interacts with the fusion proteins containing CPY* with similar efficiency, a lectin-like ERAD factor Yos9p binds to them with different efficiency. Correlation between efficiency of Yos9p interactions and ERAD of these fusion proteins indicates that Yos9p but not BiP functions in the retention of misfolded proteins for ERAD. Yos9p targets a CPY*-containing ERAD substrate to Hrd1p E3 ligase, thereby causing ER retention of the misfolded protein. This ER retention is independent of the glycan degradation signal on the misfolded protein and operates even when proteasomal degradation is inhibited. These results collectively indicate that Yos9p and Hrd1p mediate ER retention of misfolded proteins in the early stage of ERAD, which constitutes a process separable from the later degradation step.
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