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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 |
1994-11-29
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pubmed:databankReference |
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pubmed:abstractText |
To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SEC4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SSO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SSO2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptosomal-Associated Protein 25,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
79
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pubmed:geneSymbol |
SNAP25,
SNAP25A,
SNAP25B,
SSO1,
SSO2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-58
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7954793-Amino Acid Sequence,
pubmed-meshheading:7954793-Cell Membrane,
pubmed-meshheading:7954793-Exocytosis,
pubmed-meshheading:7954793-Fungal Proteins,
pubmed-meshheading:7954793-GTP-Binding Proteins,
pubmed-meshheading:7954793-Membrane Proteins,
pubmed-meshheading:7954793-Molecular Sequence Data,
pubmed-meshheading:7954793-Mutagenesis, Site-Directed,
pubmed-meshheading:7954793-Nerve Tissue Proteins,
pubmed-meshheading:7954793-Qa-SNARE Proteins,
pubmed-meshheading:7954793-Qc-SNARE Proteins,
pubmed-meshheading:7954793-R-SNARE Proteins,
pubmed-meshheading:7954793-Saccharomyces cerevisiae,
pubmed-meshheading:7954793-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:7954793-Structure-Activity Relationship,
pubmed-meshheading:7954793-Synaptosomal-Associated Protein 25,
pubmed-meshheading:7954793-rab GTP-Binding Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis.
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pubmed:affiliation |
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002.
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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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