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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1995-5-23
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pubmed:databankReference |
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pubmed:abstractText |
Over 45 VPS genes (vacuolar protein sorting) in Saccharomyces cerevisiae are necessary for the correct sorting and delivery of vacuolar hydrolases. Yeast strains carrying mutations in a subset of these VPS genes (class D vps mutants) are also defective in the segregation of vacuolar material into the developing daughter cell and are morphologically characterized by having large central vacuoles. The class D VPS gene products, which include a Rab5 homologue (VPS21/YPT51) and a syntaxin homologue (PEP12/VPS6), have been proposed to function together at a particular step along the vacuolar protein sorting pathway. We have cloned another class D VPS gene, VPS45, which is homologous to a growing family of genes that encode Sec1p-like proteins. Vps45p is predicted to be a hydrophilic protein of 577 amino acids with a molecular mass of 67 kDa. Fractionation studies show that Vps45p is a peripheral membrane protein that cofractionates with Golgi-like membranes, consistent with Vps45p functioning in membrane traffic between the Golgi and the vacuole. Using a temperature-sensitive allele of VPS45, we show that inactivation of Vps45p causes the rapid accumulation of small (40-60 nm) vesicles and secretion of the vacuolar hydrolase carboxypeptidase Y. Because the entire yeast secretory pathway is functional after the temperature-induced inactivation of Vps45p, we conclude that the accumulated vesicles represent transport intermediates between the Golgi and the vacuole.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0171-9335
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
65
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
305-18
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7720726-Amino Acid Sequence,
pubmed-meshheading:7720726-Base Sequence,
pubmed-meshheading:7720726-Biological Transport,
pubmed-meshheading:7720726-Cloning, Molecular,
pubmed-meshheading:7720726-Fungal Proteins,
pubmed-meshheading:7720726-Golgi Apparatus,
pubmed-meshheading:7720726-Liposomes,
pubmed-meshheading:7720726-Membrane Proteins,
pubmed-meshheading:7720726-Molecular Sequence Data,
pubmed-meshheading:7720726-Multigene Family,
pubmed-meshheading:7720726-Munc18 Proteins,
pubmed-meshheading:7720726-Nerve Tissue Proteins,
pubmed-meshheading:7720726-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7720726-Sequence Homology, Amino Acid,
pubmed-meshheading:7720726-Sequence Homology, Nucleic Acid,
pubmed-meshheading:7720726-Temperature,
pubmed-meshheading:7720726-Vacuoles,
pubmed-meshheading:7720726-Vesicular Transport Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Yeast Vps45p is a Sec1p-like protein required for the consumption of vacuole-targeted, post-Golgi transport vesicles.
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pubmed:affiliation |
Institute of Molecular Biology, University of Oregon, Eugene 97403-1229.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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