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Ras-GEF Cdc25p has been found to be hyperphosphorylated upon glucose addition. This work provides evidence indicating that PKA activity positively regulates the degree of Cdc25p phosphorylation, and that the intracellular association of Cdc25p and Ras2p is independent of PKA activity. In vitro experiments revealed that the Ras2-GEF activity of Cdc25p is inhibited by Cdc25p phosphorylation. These data suggest a negative feedback mechanism by which intracellular cAMP synthesis is inhibited by PKA through Cdc25p phosphorylation.
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Dong et al. (2010) studied this question.
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