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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6356
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pubmed:dateCreated |
1992-2-12
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pubmed:abstractText |
The transport of proteins destined for post-endoplasmic reticulum locations in the secretory pathway is mediated by small vesicular carriers. Transport vesicles have been generated in cell-free assays from the yeast Saccharomyces cerevisiae, and mammalian systems. Yeast genes encoding cytosolic components that participate in vesicular traffic were first identified from the collection of conditional-lethal sec-(secretory) mutants. Mutations in the yeast SEC7 gene disrupt protein transport in the secretory pathway at the nonpermissive temperature. The SEC7 gene product is a phosphoprotein of relative molecular mass 230,000 that functions from the cytoplasmic aspect of intracellular membranes. We report that in a yeast cell-free transport assay, the introduction of antibodies to Sec7 protein (Sec7p) results in the accumulation of transport vesicles. These vesicles are retrieved with Sec7p-specific antibodies by immuno-isolation for biochemical and electron microscopic characterization. Sec7p on the surface of the accumulated transport vesicles, in combination with previous genetic and biochemical studies, implicate Sec7p as part of a (non-clathrin) vesicle coat. This Sec7p-containing coat structure is proposed to be essential for vesicle budding at multiple stages in the yeast secretory pathway.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Sec7 guanine nucleotide exchange...,
http://linkedlifedata.com/resource/pubmed/chemical/mating factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
355
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
173-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1729652-Biological Transport,
pubmed-meshheading:1729652-Cell Fractionation,
pubmed-meshheading:1729652-Endoplasmic Reticulum,
pubmed-meshheading:1729652-Fungal Proteins,
pubmed-meshheading:1729652-Golgi Apparatus,
pubmed-meshheading:1729652-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:1729652-Immunosorbent Techniques,
pubmed-meshheading:1729652-Magnetics,
pubmed-meshheading:1729652-Organelles,
pubmed-meshheading:1729652-Peptides,
pubmed-meshheading:1729652-Saccharomyces cerevisiae
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pubmed:year |
1992
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pubmed:articleTitle |
Immuno-isolation of Sec7p-coated transport vesicles from the yeast secretory pathway.
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pubmed:affiliation |
Department of Cellular and Structural Biology, University of Colorado Medical School, Denver 80262.
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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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