pubmed-article:12225850 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C1752460 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C0025251 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C0032821 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C0596902 | lld:lifeskim |
pubmed-article:12225850 | lifeskim:mentions | umls-concept:C1421153 | lld:lifeskim |
pubmed-article:12225850 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:12225850 | pubmed:dateCreated | 2002-9-12 | lld:pubmed |
pubmed-article:12225850 | pubmed:abstractText | Protein kinases dedicated to the phosphorylation of SR proteins have been implicated in the processing and nuclear export of mRNAs. Here we demonstrate in Saccharomyces cerevisiae their participation in cation homeostasis. A null mutant of the single yeast SR protein kinase Sky1p is viable but exhibits increased tolerance to diverse toxic cations such as Na(+), Li(+), spermine, tetramethylammonium, hygromycin B and Mn(2+). This pleiotropic phenotype correlates with reduced accumulation of cations, suggesting a decrease in membrane electrical potential. Genetic analysis and Rb(+) uptake measurements indicate that Sky1p modulates Trk1,2, the high-affinity K(+) uptake system of yeast and a major determinant of membrane potential. | lld:pubmed |
pubmed-article:12225850 | pubmed:language | eng | lld:pubmed |
pubmed-article:12225850 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12225850 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12225850 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12225850 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12225850 | pubmed:month | Sep | lld:pubmed |
pubmed-article:12225850 | pubmed:issn | 0006-3002 | lld:pubmed |
pubmed-article:12225850 | pubmed:author | pubmed-author:FormentJavier... | lld:pubmed |
pubmed-article:12225850 | pubmed:author | pubmed-author:SerranoRamónR | lld:pubmed |
pubmed-article:12225850 | pubmed:author | pubmed-author:VicenteOscarO | lld:pubmed |
pubmed-article:12225850 | pubmed:author | pubmed-author:MuletJose MJM | lld:pubmed |
pubmed-article:12225850 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12225850 | pubmed:day | 20 | lld:pubmed |
pubmed-article:12225850 | pubmed:volume | 1565 | lld:pubmed |
pubmed-article:12225850 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12225850 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12225850 | pubmed:pagination | 36-40 | lld:pubmed |
pubmed-article:12225850 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:12225850 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12225850 | pubmed:articleTitle | The yeast SR protein kinase Sky1p modulates salt tolerance, membrane potential and the Trk1,2 potassium transporter. | lld:pubmed |
pubmed-article:12225850 | pubmed:affiliation | Dept. de Biotecnologia, Instituto de Biologi;a Molecular y Celular de Plantas, Universidad Politécnica de Valencia-CSIC, Avenida de los Naranjos s/n, Camino de Vera, 46022, Valencia, Spain | lld:pubmed |
pubmed-article:12225850 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12225850 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:855256 | entrezgene:pubmed | pubmed-article:12225850 | lld:entrezgene |
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