Phosphorylation of the S. cerevisiae Cdc25 in response to glucose results in its dissociation from Ras View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-12

AUTHORS

E Gross, D Goldberg, A Levitzki

ABSTRACT

In the yeast Sacchromyces cerevisiae, addition of glucose to starved cells triggers a transient rise in the intracellular level of cyclic AMP that induces a protein phosphorylation cascade. The glucose signal is processed by the Cdc25/Ras/adenylyl cyclase pathway, where the role of Cdc25 is to catalyse the GDP-GTP exchange on Ras. The molecular mechanisms involved in the regulation of the activity of Cdc25 are unknown. We report here the use of highly selective anti-Cdc25 antibodies to demonstrate that Cdc25 is a phospho protein and that in response to glucose it is hyperphosphorylated, within seconds, by the cyclic AMP-dependent protein kinase. It is also demonstrated that, concomitantly with hyperphosphorylation, Cdc25 partially relocalizes to the cytoplasm, reducing its accessibility to membrane-bound Ras. These results are of general significance because of the highly conserved sequence of Ras-guanyl nucleotide exchange factors from yeasts to mammals. More... »

PAGES

762

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/360762a0

DOI

http://dx.doi.org/10.1038/360762a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1009718040

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1334534


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