| pubmed-article:16390997 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16390997 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:16390997 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
| pubmed-article:16390997 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:16390997 | lifeskim:mentions | umls-concept:C0024054 | lld:lifeskim |
| pubmed-article:16390997 | lifeskim:mentions | umls-concept:C0752065 | lld:lifeskim |
| pubmed-article:16390997 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16390997 | pubmed:dateCreated | 2006-1-4 | lld:pubmed |
| pubmed-article:16390997 | pubmed:abstractText | Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation. | lld:pubmed |
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| pubmed-article:16390997 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16390997 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16390997 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16390997 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16390997 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:16390997 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:NovickPeterP | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:YatesJohn... | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:GangarAkanksh... | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:NiessenSherry... | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:BrennwaldPatr... | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:AndreevaAnnaA | lld:pubmed |
| pubmed-article:16390997 | pubmed:author | pubmed-author:GrosshansBian... | lld:pubmed |
| pubmed-article:16390997 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16390997 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:16390997 | pubmed:volume | 172 | lld:pubmed |
| pubmed-article:16390997 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16390997 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16390997 | pubmed:pagination | 55-66 | lld:pubmed |
| pubmed-article:16390997 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:16390997 | pubmed:meshHeading | pubmed-meshheading:16390997... | lld:pubmed |
| pubmed-article:16390997 | pubmed:meshHeading | pubmed-meshheading:16390997... | lld:pubmed |
| pubmed-article:16390997 | pubmed:meshHeading | pubmed-meshheading:16390997... | lld:pubmed |
| pubmed-article:16390997 | pubmed:meshHeading | pubmed-meshheading:16390997... | lld:pubmed |
