Abstract
Ycf1p function is regulated by casein kinase 2α, Cka1p, via phosphorylation of Ser251. Cka1p-mediated phosphorylation of Ycf1p is attenuated in response to high salt stress. Previous results from our lab suggest a role for Ycf1p in cellular resistance to salt stress. Here, we show that Ycf1p plays an important role in cellular resistance to salt stress by maintaining the cellular redox balance via glutathione recycling. Our results suggest that during acute salt stress increased Sod1p, Sod2p and Ctt1p activity is the main compensatory for the loss in Ycf1p function that results from reduced Ycf1p-dependent recycling of cellular GSH levels.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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ATP-Binding Cassette Transporters / genetics
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ATP-Binding Cassette Transporters / metabolism*
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Animals
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Biomarkers / metabolism
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Casein Kinase II / metabolism
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Glutathione / metabolism
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Hydrogen Peroxide / pharmacology
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Oxidants / pharmacology
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Oxidation-Reduction
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Oxidative Stress*
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Phosphorylation
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Saccharomyces cerevisiae / drug effects
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Salts / pharmacology*
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Superoxide Dismutase / genetics
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Superoxide Dismutase / metabolism
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Superoxide Dismutase-1
Substances
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ATP-Binding Cassette Transporters
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Biomarkers
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Oxidants
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Saccharomyces cerevisiae Proteins
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Salts
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YCF1 protein, S cerevisiae
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Hydrogen Peroxide
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Superoxide Dismutase
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Superoxide Dismutase-1
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superoxide dismutase 2
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Casein Kinase II
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Glutathione