Linked Life Data

16926153

Source:http://linkedlifedata.com/resource/pubmed/id/16926153

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
42
pubmed:dateCreated
2006-10-16
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32025-35
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16926153-Amino Acid Sequence, pubmed-meshheading:16926153-Cloning, Molecular, pubmed-meshheading:16926153-Endoplasmic Reticulum, pubmed-meshheading:16926153-Fungal Proteins, pubmed-meshheading:16926153-Gene Deletion, pubmed-meshheading:16926153-Intracellular Membranes, pubmed-meshheading:16926153-Membrane Proteins, pubmed-meshheading:16926153-Molecular Chaperones, pubmed-meshheading:16926153-Molecular Sequence Data, pubmed-meshheading:16926153-Mutation, pubmed-meshheading:16926153-Protein Conformation, pubmed-meshheading:16926153-Protein Structure, Tertiary, pubmed-meshheading:16926153-Saccharomyces cerevisiae, pubmed-meshheading:16926153-Saccharomyces cerevisiae Proteins, pubmed-meshheading:16926153-Sequence Homology, Amino Acid, pubmed-meshheading:16926153-Vacuolar Proton-Translocating ATPases, pubmed-meshheading:16926153-Vacuoles
pubmed:year
2006
pubmed:articleTitle
PKR1 encodes an assembly factor for the yeast V-type ATPase.
pubmed:affiliation
Division of Immunology and Cell Biology, Department of Pathology, School of Medicine, University of Utah, Salt Lake City, Utah 84132-2501, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural