Linked Life Data

16185821

Source:http://linkedlifedata.com/resource/pubmed/id/16185821

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2005-10-28
pubmed:databankReference
pubmed:abstractText
The highly conserved exocyst complex of eukaryotic cells allows the polarized transport and fusion of late secretory vesicles with the plasma membrane. In Saccharomyces cerevisiae the Sec6p component of the exocyst complex is essential for cell growth. The sec6-4 temperature-sensitive mutation of the S. cerevisiae SEC6 gene leads to the accumulation of large amounts of mature late post-Golgi secretory vesicles in the cytosol of mutant cells at the restrictive temperature of 37 degrees C. These readily isolated, inside-out and tightly sealed vesicles contain mature post-translationally modified plasma membrane and secretory proteins and provide a valuable tool for the study of plasma membrane protein function. This study shows that the single point mutation L633P in the SEC6 coding region defines the sec6-4 phenotype. We followed the localization of the wild type Sec6p and the mutant Sec6-4p proteins (C-terminally tagged with the green fluorescent protein yEGfp3p) in the presence or absence of heterologously over-expressed Candida albicans plasma membrane ATP-binding cassette (ABC) transporter CaCdr1p (C-terminally tagged with the red fluorescent protein mRfp1p). The Sec6-4p protein localized to buds and septa, like wild type Sec6p, at the permissive temperature of 23 degrees C and the sec6-4 mutant cells grew at the same rate as the wild type control cells. Sec6-4p was mislocalized at the restrictive temperature of 37 degrees C and heterogenous vesicles accumulated in cells but sec6-4 cells also accumulated homogenous secretory vesicles at the permissive temperature.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
361
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-66
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:16185821-ATP-Binding Cassette Transporters, pubmed-meshheading:16185821-Alleles, pubmed-meshheading:16185821-Candida albicans, pubmed-meshheading:16185821-Carrier Proteins, pubmed-meshheading:16185821-Green Fluorescent Proteins, pubmed-meshheading:16185821-Luminescent Proteins, pubmed-meshheading:16185821-Microscopy, Confocal, pubmed-meshheading:16185821-Microscopy, Electron, Transmission, pubmed-meshheading:16185821-Molecular Sequence Data, pubmed-meshheading:16185821-Phenotype, pubmed-meshheading:16185821-Plasmids, pubmed-meshheading:16185821-Point Mutation, pubmed-meshheading:16185821-Recombinant Fusion Proteins, pubmed-meshheading:16185821-Saccharomyces cerevisiae, pubmed-meshheading:16185821-Saccharomyces cerevisiae Proteins, pubmed-meshheading:16185821-Temperature, pubmed-meshheading:16185821-Transformation, Genetic, pubmed-meshheading:16185821-Vesicular Transport Proteins
pubmed:year
2005
pubmed:articleTitle
Characterization of the Saccharomyces cerevisiae sec6-4 mutation and tools to create S. cerevisiae strains containing the sec6-4 allele.
pubmed:affiliation
University of Otago, Department of Oral Sciences, PO Box 647, Dunedin 9001, New Zealand. erwin.lamping@stonebow.otago.ac.nz
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't