Format

Send to

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

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

Author information

1
Departamento de Bioquímica and Instituto de Investigaciones Biomédicas 'Alberto Sols', Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid, Arturo Duperier, 4, 28029 Madrid, Spain.
2
Departamento de Bioquímica and Instituto de Investigaciones Biomédicas 'Alberto Sols', Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid, Arturo Duperier, 4, 28029 Madrid, Spain fportillo@iib.uam.es.

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

PMID:
26019146
DOI:
10.1093/femsyr/fov030
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center