| pubmed-article:1569938 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C1325417 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0018353 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0032214 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C0600138 | lld:lifeskim |
| pubmed-article:1569938 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:1569938 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:1569938 | pubmed:dateCreated | 1992-5-27 | lld:pubmed |
| pubmed-article:1569938 | pubmed:abstractText | Sec4, a GTP-binding protein of the ras superfamily, is required for exocytosis in the budding yeast Saccharomyces cerevisiae. To test the role of GTP hydrolysis in Sec4 function, we constructed a mutation, Q-79----L, analogous to the oncogenic mutation of Q-61----L in Ras, in a region of Sec4 predicted to interact with the phosphoryl group of GTP. The sec4-leu79 mutation lowers the intrinsic hydrolysis rate to unmeasurable levels. A component of a yeast lysate specifically stimulates the hydrolysis of GTP by Sec4, while the rate of hydrolysis of GTP by Sec4-Leu79 can be stimulated by this GAP activity to only 30% of the stimulated hydrolysis rate of the wild-type protein. The decreased rate of hydrolysis results in the accumulation of the Sec4-Leu79 protein in its GTP-bound form in an overproducing yeast strain. The sec4-leu79 allele can function as the sole copy of sec4 in yeast cells. However, it causes recessive, cold-sensitive growth, a slowing of invertase secretion, and accumulation of secretory vesicles and displays synthetic lethality with a subset of other secretory mutants, indicative of a partial loss of Sec4 function. While the level of Ras function reflects the absolute level of GTP-bound protein, our results suggest that the ability of Sec4 to cycle between its GTP and GDP bound forms is important for its function in vesicular transport, supporting a mechanism for Sec4 function which is distinct from that of the Ras protein. | lld:pubmed |
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| pubmed-article:1569938 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1569938 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1569938 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1569938 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1569938 | pubmed:month | May | lld:pubmed |
| pubmed-article:1569938 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1569938 | pubmed:author | pubmed-author:NovickPP | lld:pubmed |
| pubmed-article:1569938 | pubmed:author | pubmed-author:GarrettMM | lld:pubmed |
| pubmed-article:1569938 | pubmed:author | pubmed-author:KabcenellA... | lld:pubmed |
| pubmed-article:1569938 | pubmed:author | pubmed-author:BrennwaldPP | lld:pubmed |
| pubmed-article:1569938 | pubmed:author | pubmed-author:WalworthN CNC | lld:pubmed |
| pubmed-article:1569938 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1569938 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:1569938 | pubmed:geneSymbol | ras | lld:pubmed |
| pubmed-article:1569938 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1569938 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1569938 | pubmed:pagination | 2017-28 | lld:pubmed |
| pubmed-article:1569938 | pubmed:dateRevised | 2010-9-7 | lld:pubmed |
| pubmed-article:1569938 | pubmed:meshHeading | pubmed-meshheading:1569938-... | lld:pubmed |
| pubmed-article:1569938 | pubmed:meshHeading | pubmed-meshheading:1569938-... | lld:pubmed |
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| pubmed-article:1569938 | pubmed:meshHeading | pubmed-meshheading:1569938-... | lld:pubmed |
