Source:http://linkedlifedata.com/resource/pubmed/id/15164360
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2004-5-27
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pubmed:abstractText |
Trk, encoded by the partially redundant genes TRK1 and TRK2, is the major potassium transporter of Saccharomyces cerevisiae. This system is specific for potassium and rubidium but, by reducing the electrical membrane potential of the plasma membrane, Trk decreases the uptake of toxic cations such as lithium, calcium, aminoglycosides and polyamines, which are transported by other systems. Gain- and loss-of-function studies indicate that TPS1, a gene encoding trehalose-6-phosphate synthase and known to modulate glucose metabolism, activates Trk and reduces the sensitivity of yeast cells to many toxic cations. This effect is independent of known regulators of Trk, such as the Hal4 and Hal5 protein kinases and the protein phosphatase calcineurin. Mutants defective in isoform 2 of phosphoglucomutase (pgm2) and mutants defective in isoform 2 of hexokinase (hxk2) exhibit similar phenotypes of reduced Trk activity and increased sensitivity to toxic cations compared with tps1 mutants. In all cases Trk activity was positively correlated with levels of glucose phosphates (glc-1-P and glc-6-P). These results indicate that Tps1, like Pgm2 and Hxk2, increases the levels of glucose phosphates and suggest that these metabolites, directly or indirectly, activate Trk.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosephosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Lithium,
http://linkedlifedata.com/resource/pubmed/chemical/Potassium,
http://linkedlifedata.com/resource/pubmed/chemical/Rubidium,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trehalose,
http://linkedlifedata.com/resource/pubmed/chemical/trehalose-6-phosphate synthase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0749-503X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2004 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
569-82
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15164360-Adenosine Triphosphatases,
pubmed-meshheading:15164360-Biological Transport,
pubmed-meshheading:15164360-Cation Transport Proteins,
pubmed-meshheading:15164360-Glucosephosphates,
pubmed-meshheading:15164360-Glucosyltransferases,
pubmed-meshheading:15164360-Lithium,
pubmed-meshheading:15164360-Potassium,
pubmed-meshheading:15164360-Rubidium,
pubmed-meshheading:15164360-Saccharomyces cerevisiae,
pubmed-meshheading:15164360-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15164360-Trehalose
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pubmed:year |
2004
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pubmed:articleTitle |
The trehalose pathway and intracellular glucose phosphates as modulators of potassium transport and general cation homeostasis in yeast.
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pubmed:affiliation |
Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-CSIC, Camino de Vera, 46022 Valencia, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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