Other names published for PRC1: LBC1, CPY, carboxypeptidase C PRC1, YMR297W
PRC1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Cellular Location
- Function/Process
- Genetic Interactions
- Mutants/Phenotypes
- Regulation of
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PRC1 - Mutants/Phenotypes (63)
| Reference | Other Genes Addressed |
|---|---|
| Hsu CL, et al. (2012) Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways. Mol Biol Cell 23(4):630-41 | |
| Izawa T, et al. (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93 | |
| Wheeler MC and Gekakis N (2012) Defective ER associated degradation of a model luminal substrate in yeast carrying a mutation in the 4th ER luminal loop of Sec61p. Biochem Biophys Res Commun 427(4):768-73 | |
| Arlt H, et al. (2011) An overexpression screen in Saccharomyces cerevisiae identifies novel genes that affect endocytic protein trafficking. Traffic 12(11):1592-603 | |
| Benitez EM, et al. (2011) Yos9, a control protein for misfolded glycosylated and non-glycosylated proteins in ERAD. FEBS Lett 585(19):3015-9 | |
| Forte GM, et al. (2011) N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol 9(5):e1001073 | |
| Gardner BM and Walter P (2011) Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333(6051):1891-4 | |
| Brown CR, et al. (2010) The TOR complex 1 is distributed in endosomes and in retrograde vesicles that form from the vacuole membrane and plays an important role in the vacuole import and degradation pathway. J Biol Chem 285(30):23359-70 | |
| Esposito AM and Kinzy TG (2010) The Eukaryotic Translation Elongation Factor 1B{gamma} Has a Non-guanine Nucleotide Exchange Factor Role in Protein Metabolism. J Biol Chem 285(49):37995-8004 | |
| Junne T, et al. (2010) The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration. Mol Biol Cell 21(10):1662-70 | |
| Kanehara K, et al. (2010) Modularity of the Hrd1 ERAD complex underlies its diverse client range. J Cell Biol 188(5):707-16 | |
| Kawaguchi S, et al. (2010) Interplay of substrate retention and export signals in endoplasmic reticulum quality control. PLoS One 5(11):e15532 | |
| Prosser DC, et al. (2010) Quantitative Analysis of Endocytosis with Cytoplasmic pHluorin Chimeras. Traffic 11(9):1141-50 | |
| Spedale G, et al. (2010) Identification of Pep4p as the protease responsible for formation of the SAGA-related SLIK protein complex. J Biol Chem 285(30):22793-9 | |
| Wunschmann J, et al. (2010) Dissection of glutathione conjugate turnover in yeast. Phytochemistry 71(1):54-61 | |
| Metzger MB and Michaelis S (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19 | |
| Schafer A and Wolf DH (2009) Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J 28(19):2874-84 | |
| Xie W, et al. (2009) Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system. Mol Biol Cell 20(14):3317-29 | |
| Liu Y and Chang A (2008) Heat shock response relieves ER stress. EMBO J 27(7):1049-59 | |
| Merksamer PI, et al. (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135(5):933-47 | |
| Willer M, et al. (2008) Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY. J Biol Chem 283(49):33883-8 | |
| Ganguli D, et al. (2007) The Alternative Pathway of Glutathione Degradation Is Mediated by a Novel Protein Complex Involving Three New Genes in Saccharomyces cerevisiae. Genetics 175(3):1137-51 | |
| Kincaid MM and Cooper AA (2007) Misfolded proteins traffic from the endoplasmic reticulum (ER) due to ER export signals. Mol Biol Cell 18(2):455-63 | |
| Kodama H, et al. (2007) The role of N-terminal domain of translational release factor eRF3 for the control of functionality and stability in S. cerevisiae. Genes Cells 12(5):639-50 | |
| Okochi N, et al. (2007) Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface. Appl Microbiol Biotechnol 77(3):597-603 | |
| Wunschmann J, et al. (2007) Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae. FEBS Lett 581(8):1681-7 | |
| Kostova Z and Wolf DH (2005) Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. J Cell Sci 118(Pt 7):1485-92 | |
| Spear ED and Ng DT (2005) Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J Cell Biol 169(1):73-82 | |
| Szathmary R, et al. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19(6):765-75 | |
| Haynes CM, et al. (2004) Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death. Mol Cell 15(5):767-76 |





