Abstract
In this study we show that Reg1, the regulatory subunit of the Reg1/Glc7 protein phosphatase (PP1) complex, interacts physically with the two yeast members of the 14-3-3 protein family, Bmh1 and Bmh2. By using different fragments of the Reg1 protein we mapped the interaction domain at the N-terminal part of the protein. We also show that Reg1 and yeast 14-3-3 proteins participate actively in the regulation of the glucose-induced degradation of maltose permease (Mal61).
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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14-3-3 Proteins
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Enzyme Inhibitors / pharmacology
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Immunoblotting
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Membrane Transport Modulators*
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Membrane Transport Proteins / antagonists & inhibitors*
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Models, Genetic
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Monosaccharide Transport Proteins / genetics
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Monosaccharide Transport Proteins / metabolism*
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Oligonucleotides / chemistry
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Protein Binding
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Symporters / genetics
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Symporters / metabolism*
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Temperature
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Time Factors
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Two-Hybrid System Techniques
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Tyrosine 3-Monooxygenase / metabolism*
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beta-Galactosidase / metabolism
Substances
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14-3-3 Proteins
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BMH1 protein, S cerevisiae
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BMH2 protein, S cerevisiae
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Enzyme Inhibitors
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Membrane Transport Modulators
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Membrane Transport Proteins
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Monosaccharide Transport Proteins
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Oligonucleotides
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Saccharomyces cerevisiae Proteins
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Symporters
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maltose transport system, S cerevisiae
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maltose permease
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Tyrosine 3-Monooxygenase
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beta-Galactosidase