pubmed-article:18357452 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0085403 | lld:lifeskim |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0011155 | lld:lifeskim |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:18357452 | lifeskim:mentions | umls-concept:C0683598 | lld:lifeskim |
pubmed-article:18357452 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:18357452 | pubmed:dateCreated | 2008-4-11 | lld:pubmed |
pubmed-article:18357452 | pubmed:abstractText | Resistance to thiol oxidation can arise from mutations altering redox homeostasis. A Saccharomyces cerevisiae sit4-110 mutant is here described, which was isolated as resistant to the thiol-specific oxidant dipyridyl disulfide (DPS) and which contains a single-residue substitution in the SIT4 gene. Sit4p is a protein phosphatase with multiple roles in signal transduction through the target-of-rapamycin (TOR) pathway. We found that sit4-110 elevates the levels of glutathione. However, this cannot be the (only) cause for the DPS-resistance, since sit4-110 also conferred DPS/H2O2-resistance in a glutathione-deficient strain. Of the known Sit4p substrates, only Tip41p is involved in DPS-resistance; both Delta tip41 deletion and overexpression of the Tip41p target Tap42p resulted in increased DPS-resistance. Thus, the role of Sit4p in DPS-tolerance differs from its role during TOR-inactivation and salt stress. In view of Tap42p's known involvement in actin homeostasis, sit4-110 could compensate for putative actin-related defects caused by DPS. However, sit4-110 has pronounced actin polarization defects under both absence and presence of DPS. A relation between actin homeostasis and DPS resistance of sit4-110 cannot be ruled out, but our results suggest that unknown pathways might be involved in DPS resistance through mechanisms involving the Sit4p and/or Tap42p function(s). | lld:pubmed |
pubmed-article:18357452 | pubmed:language | eng | lld:pubmed |
pubmed-article:18357452 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18357452 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18357452 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18357452 | pubmed:month | May | lld:pubmed |
pubmed-article:18357452 | pubmed:issn | 0172-8083 | lld:pubmed |
pubmed-article:18357452 | pubmed:author | pubmed-author:WintherJakob... | lld:pubmed |
pubmed-article:18357452 | pubmed:author | pubmed-author:Kielland-Bran... | lld:pubmed |
pubmed-article:18357452 | pubmed:author | pubmed-author:López-Mirabal... | lld:pubmed |
pubmed-article:18357452 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18357452 | pubmed:volume | 53 | lld:pubmed |
pubmed-article:18357452 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18357452 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18357452 | pubmed:pagination | 275-86 | lld:pubmed |
pubmed-article:18357452 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:18357452 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18357452 | pubmed:articleTitle | Oxidant resistance in a yeast mutant deficient in the Sit4 phosphatase. | lld:pubmed |
pubmed-article:18357452 | pubmed:affiliation | Carlsberg Laboratory, Gamle Carlsberg Vej 10, 2500 Copenhagen Valby, Denmark. | lld:pubmed |
pubmed-article:18357452 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18357452 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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