Specific phosphoantibodies reveal two phosphorylation sites in yeast Pma1 in response to glucose

FEMS Yeast Res. 2015 Aug;15(5):fov030. doi: 10.1093/femsyr/fov030. Epub 2015 May 27.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Antibodies / immunology
  • Enzyme Activation
  • Glucose / metabolism*
  • Membrane Proteins / metabolism
  • Phosphorylation
  • Protein Phosphatase 1 / genetics
  • Protein Phosphatase 1 / metabolism*
  • Protein Processing, Post-Translational / genetics
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Antibodies
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • Adenosine Triphosphate
  • GLC7 protein, S cerevisiae
  • Protein Phosphatase 1
  • PMA1 protein, S cerevisiae
  • Proton-Translocating ATPases
  • Glucose