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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
1995-6-1
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pubmed:abstractText |
Saccharomyces cerevisiae VMA genes, encoding essential components for the expression of vacuolar membrane H(+)-ATPase activity, are involved in intracellular ionic homeostasis and vacuolar biogenesis. We report here that the immunosuppressants FK506 and cyclosporin A cause general growth inhibition of the vma3 mutant. Upon addition of the drugs, the mutant grew neither in the presence of more than 5 mM Ca2+ nor above pH 6.0. The action of the immunosuppressants is dependent on their binding proteins and ascribable to inhibition of calcineurin activity; a mutation of a calcineurin subunit (cnb1) shows synthetic lethal interaction with the vma mutation. The addition of FK506 decreases the cytosolic free concentration of Ca2+ in the vma3 mutant cells. Consequently, FK506 induces an 8.9-fold elevation of a nonexchangeable Ca2+ pool. These results suggest that calcineurin controls calcium homeostasis by repression of Ca2+ flux into a cellular compartment(s) and that the vacuolar H(+)-ATPase is essential for cell growth cooperating with calcineurin to regulate the cytosolic free concentration of Ca2+.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcineurin,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporine,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus,
http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10113-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7537264-Base Sequence,
pubmed-meshheading:7537264-Calcineurin,
pubmed-meshheading:7537264-Calcium,
pubmed-meshheading:7537264-Calmodulin-Binding Proteins,
pubmed-meshheading:7537264-Carrier Proteins,
pubmed-meshheading:7537264-Cell Division,
pubmed-meshheading:7537264-Cyclosporine,
pubmed-meshheading:7537264-DNA Primers,
pubmed-meshheading:7537264-DNA-Binding Proteins,
pubmed-meshheading:7537264-Heat-Shock Proteins,
pubmed-meshheading:7537264-Homeostasis,
pubmed-meshheading:7537264-Hydrogen-Ion Concentration,
pubmed-meshheading:7537264-Intracellular Membranes,
pubmed-meshheading:7537264-Molecular Sequence Data,
pubmed-meshheading:7537264-Mutation,
pubmed-meshheading:7537264-Phosphoprotein Phosphatases,
pubmed-meshheading:7537264-Proton-Translocating ATPases,
pubmed-meshheading:7537264-Saccharomyces cerevisiae,
pubmed-meshheading:7537264-Tacrolimus,
pubmed-meshheading:7537264-Tacrolimus Binding Proteins,
pubmed-meshheading:7537264-Vacuoles
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pubmed:year |
1995
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pubmed:articleTitle |
Cooperation of calcineurin and vacuolar H(+)-ATPase in intracellular Ca2+ homeostasis of yeast cells.
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pubmed:affiliation |
Department of Plant Sciences, Graduate School of Science, University of Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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