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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Yeast protein kinase Ptk2 localizes at the plasma membrane and phosphorylates in vitro the C-terminal peptide of the H+-ATPase.

Glucose triggers posttranslational modifications that increase the activity of the Saccharomyces cerevisiae plasma membrane H+-ATPase (Pma1). Glucose activation of yeast H+-ATPase results from the change in two kinetic parameters: an increase in the affinity of the enzyme for ATP, depending on Ser899, and an increase in the Vmax involving Thr912. Our previous studies suggested that Ptk2 mediates the Ser899-dependent part of the activation. In this study we find that Ptk2 localized to the plasma membrane in a Triton X-100 insoluble fraction. In vitro phosphorylation assays using a recombinant GST-fusion protein comprising 30 C-terminal amino acids of Pma1 suggest that Ser899 is phosphorylated by Ptk2. Furthermore, we show that the Ptk2 carboxyl terminus is essential for glucose-dependent Pma1 activation and for the phosphorylation of Ser899.[1]

References

  1. Yeast protein kinase Ptk2 localizes at the plasma membrane and phosphorylates in vitro the C-terminal peptide of the H+-ATPase. Eraso, P., Mazón, M.J., Portillo, F. Biochim. Biophys. Acta (2006) [Pubmed]
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