Abstract
Glucose triggers post-translational modifications of the Saccharomyces cerevisiae plasma membrane H(+)-ATPase (Pma1) that lead to an increase in enzyme activity. The activation results from changes in two kinetic parameters: an increase in the affinity of the enzyme for ATP, depending on Ser899, and an increase in the Vmax involving Ser911/Thr912. Using phosphospecific antibodies, we show that Ser899 and Ser911/Thr912 are phosphorylated in vivo during glucose activation and that protein phosphatase Glc7 is involved in the dephosphorylation of Ser899 upon glucose starvation.
Keywords:
Pma1; glucose activation; phosphorylation; yeast.
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Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism*
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Antibodies / immunology
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Enzyme Activation
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Glucose / metabolism*
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Membrane Proteins / metabolism
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Phosphorylation
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Protein Phosphatase 1 / genetics
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Protein Phosphatase 1 / metabolism*
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Protein Processing, Post-Translational / genetics
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Proton-Translocating ATPases / genetics
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Proton-Translocating ATPases / metabolism*
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
Substances
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Antibodies
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Membrane Proteins
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Saccharomyces cerevisiae Proteins
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Adenosine Triphosphate
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GLC7 protein, S cerevisiae
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Protein Phosphatase 1
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PMA1 protein, S cerevisiae
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Proton-Translocating ATPases
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Glucose