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J. Biol. Chem. Oct (2006); 281(42):32025-35
PKR1 encodes an assembly factor for the yeast V-type ATPase-
Davis-Kaplan SR, Compton MA, Flannery AR, Ward DM, Kaplan J, Stevens TH, Graham LA
Division of Immunology and Cell Biology, Department of Pathology, School of Medicine, University of Utah, Salt Lake City, Utah 84132-2501, USA-
Abstract: Deletion of the yeast gene PKR1 -YMR123W- results in an inability to grow on iron-limited medium- Pkr1p is localized to the membrane of the endoplasmic reticulum- Cells lacking Pkr1p show reduced levels of the V-ATPase subunit Vph1p due to increased turnover of the protein in mutant cells- Reduced levels of the V-ATPase lead to defective copper loading of Fet3p, a component of the high affinity iron transport system- Levels of Vph1p in cells lacking Pkr1p are similar to cells unable to assemble a functional V-ATPase due to lack of a V0 subunit or an endoplasmic reticulum -ER- assembly factor- However, unlike yeast mutants lacking a V0 subunit or a V-ATPase assembly factor, low levels of Vph1p present in cells lacking Pkr1p are assembled into a V-ATPase complex, which exits the ER and is present on the vacuolar membrane- The V-ATPase assembled in the absence of Pkr1p is fully functional because the mutant cells are able to weakly acidify their vacuoles- Finally, overexpression of the V-ATPase assembly factor Vma21p suppresses the growth and acidification defects of pkr1Delta cells- Our data indicate that Pkr1p functions together with the other V-ATPase assembly factors in the ER to efficiently assemble the V-ATPase membrane sector-
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.