| pubmed-article:7954793 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
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| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C0015283 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C1420270 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:7954793 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:7954793 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:7954793 | pubmed:dateCreated | 1994-11-29 | lld:pubmed |
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| pubmed-article:7954793 | 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. | lld:pubmed |
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| pubmed-article:7954793 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7954793 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7954793 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7954793 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7954793 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:BankaitisVV | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:NovickPP | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:KeränenSS | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:BrennwaldPP | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:KearnsBB | lld:pubmed |
| pubmed-article:7954793 | pubmed:author | pubmed-author:ChampiotMM | lld:pubmed |
| pubmed-article:7954793 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7954793 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:7954793 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:7954793 | pubmed:geneSymbol | SNAP25 | lld:pubmed |
| pubmed-article:7954793 | pubmed:geneSymbol | SSO2 | lld:pubmed |
| pubmed-article:7954793 | pubmed:geneSymbol | SSO1 | lld:pubmed |
| pubmed-article:7954793 | pubmed:geneSymbol | SNAP25A | lld:pubmed |
| pubmed-article:7954793 | pubmed:geneSymbol | SNAP25B | lld:pubmed |
| pubmed-article:7954793 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7954793 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7954793 | pubmed:pagination | 245-58 | lld:pubmed |
| pubmed-article:7954793 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7954793 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7954793 | pubmed:articleTitle | Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. | lld:pubmed |
| pubmed-article:7954793 | pubmed:affiliation | Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8002. | lld:pubmed |
| pubmed-article:7954793 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7954793 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7954793 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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