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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1997-3-6
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| pubmed:databankReference | |
| pubmed:abstractText |
We have cloned the gene, vps34+, from the fission yeast Schizosaccharomyces pombe which encodes an 801 amino acid protein with phosphatidylinositol 3-kinase activity. The S. pombe Vps34 protein shares 43% amino acid sequence identity with the Saccharomyces cerevisiae Vps34 protein and 28% identity with the p110 catalytic subunit of the mammalian phosphatidylinositol 3-kinase. When the vps34+ gene is disrupted, S.pombe strains are temperature-sensitive for growth and the mutant cells contain enlarged vacuoles. Furthermore, while wild-type strains exhibit substantial levels of phosphatidylinositol 3-kinase activity, this activity is not detected in the vps34 delta strain. S.pombe Vps34p-specific antiserum detects a single protein in cells of -90 kDa that fractionates almost exclusively with the crude membrane fraction. Phosphatidylinositol 3-kinase activity also is localized mainly in the membrane fraction of wild-type cells. Immunoisolated Vps34p specifically phosphorylates phosphatidylinositol on the D-3 position of the inositol ring to yield phosphatidylinositol(3)phosphate. but does not utilize phosphatidylinositol(4)phosphate or phosphatidylinositol(4,5)bisphosphate as substrates. In addition, when compared to the mammalian p110 phosphatidylinositol 3-kinase, S. pombe Vps34p is relatively insensitive to the inhibitors wortmannin and LY294002. Together, these results indicate that S. pombe Vps34 is more similar to the phosphatidylinositol-specific 3-kinase, Vps34p from S. cerevisiae, and is distinct from the p110/p85 and G protein-coupled phosphatidylinositol 3-kinases from mammalian cells. These data are discussed in relation to the possible role of Vps34p in vesicle-mediated protein sorting to the S. pombe vacuole.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
|
| pubmed:issn |
0021-9533
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
108 ( Pt 12)
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3745-56
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:8719881-Amino Acid Sequence,
pubmed-meshheading:8719881-Base Sequence,
pubmed-meshheading:8719881-Cell Division,
pubmed-meshheading:8719881-Cloning, Molecular,
pubmed-meshheading:8719881-Genes, Fungal,
pubmed-meshheading:8719881-Molecular Sequence Data,
pubmed-meshheading:8719881-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:8719881-Phosphatidylinositols,
pubmed-meshheading:8719881-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8719881-Polymerase Chain Reaction,
pubmed-meshheading:8719881-Reference Values,
pubmed-meshheading:8719881-Saccharomyces cerevisiae,
pubmed-meshheading:8719881-Schizosaccharomyces,
pubmed-meshheading:8719881-Species Specificity,
pubmed-meshheading:8719881-Substrate Specificity,
pubmed-meshheading:8719881-Vacuoles
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Schizosaccharomyces pombe Vps34p, a phosphatidylinositol-specific PI 3-kinase essential for normal cell growth and vacuole morphology.
|
| pubmed:affiliation |
Division of Cellular and Molecular Medicine, University of California, San Diego, School of Medicine, La Jolla, CA 92093-0668, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|