Open AccessThe localization and concentration of the PDE2 ‐encoded high‐affinity cAMP phosphodiesterase is regulated by cAMP‐dependent protein kinase A in the yeast Saccharomyces cerevisiae
Author(s) -
Hu Yun,
Liu Enkai,
Bai Xiaojia,
Zhang Aili
Publication year - 2010
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2009.00598.x
Subject(s) - biology , protein kinase a , saccharomyces cerevisiae , phosphodiesterase , phosphodiesterase 3 , biochemistry , yeast , microbiology and biotechnology , cytoplasm , intracellular , kinase , enzyme
The genome of the yeast Saccharomyces cerevisiae encodes two cyclic AMP (cAMP) phosphodiesterases, a low‐affinity one, Pde1, and a high‐affinity one, Pde2. Pde1 has been ascribed a function for downregulating agonist‐induced cAMP accumulation in a protein kinase A (PKA)‐governed negative feedback loop, whereas Pde2 controls the basal cAMP level in the cell. Here we show that PKA regulates the localization and protein concentration of Pde2. Pde2 is accumulated in the nucleus in wild‐type cells growing on glucose, or in strains with hyperactive PKA. In contrast, in derepressed wild‐type cells or cells with attenuated PKA activity, Pde2 is distributed over the nucleus and cytoplasm. We also show evidence indicating that the Pde2 protein level is positively correlated with PKA activity. The increase in the Pde2 protein level in high‐PKA strains and in cells growing on glucose was due to its increased half‐life. These results suggest that, like its low‐affinity counterpart, the high‐affinity phosphodiesterase may also play an important role in the PKA‐controlled feedback inhibition of intracellular cAMP.