Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

Nikawa, Jùn‐ichi; Sass, Philip M.; Wigler, Michael

doi:10.1128/mcb.7.10.3629

Cited by 207 publications

(168 citation statements)

References 40 publications

Supporting

Mentioning

164

Contrasting

Order By: Relevance

“…PKA itself is involved in this mechanism since basal cAMP levels are dramatically increased in strains with reduced activity of the kinase (Nikawa et al 1987a;Mbonyi et al 1990). cAMP is hydrolyzed by the low-and high-affinity phosphodiesterases, respectively, encoded by PDE1 and PDE2 (Sass et al 1986;Nikawa et al 1987b;Wilson and Tatchell 1988). The high-affinity phosphodiesterase Pde2 appears to control basal cAMP levels, which is important to prevent undesirable PKA activity during stationary phase (Park et al 2005).…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

View full text Add to dashboard Cite

Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

show abstract

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Because deletion of GPR1 or GPA2 reduces glucose-induced cAMP signaling, the observed enhancement of Ras-GTP loading is not sufficient for full glucose-induced stimulation of cAMP synthesis (Colombo et al, 2004). The cAMP level is also controlled by a low and a high-affinity phosphodiesterase, respectively, encoded by PDE1 and PDE2 (Nikawa, Sass, & Wigler, 1987;Sass, Field, Nikawa, Toda, & Wigler, 1986).…”

Section: Introductionmentioning

confidence: 99%

In Saccharomyces cerevisiae an unbalanced level of tyrosine phosphorylation down-regulates the Ras/PKA pathway

Magherini

Busti

Gamberi

et al. 2006

The International Journal of Biochemistry & Cell Biology

View full text Add to dashboard Cite

The role of tyrosyl phosphorylation/dephosphorylation in the budding yeast Saccharomyces cerevisiae, whose genome does not encode typical tyrosyne kinases, has long remained elusive. Nevertheless, several protein kinases phosphorylating poly(TyrGlu) substrates have been identified. In this work, we use the expression of the low molecular weight tyrosine phosphatase Stp1 from the distantly related yeast Schizosaccharomyces pombe, as a tool to investigate whether an unbalanced level of protein tyrosine phosphorylation affects S. cerevisiae growth and metabolism. We correlate the previously reported down-regulation of the phosphotyrosine level brought about by overexpression of Stp1 with a large number of phenotypes indicative of down-regulation of the Ras pathway. These phenotypes include reduction in both glucose-and acidification-induced GTP loading of the Ras2 protein and cAMP signaling, impaired growth on a non-fermentable carbon source, alteration of cell cycle parameters, delayed recovery from nitrogen starvation, increased heat-shock resistance, attenuated pseudohyphal and invasive growth. Genetic data suggest that Stp1 acts either at, or above, the level of Ras2, possibly on the Ira proteins. Consistently, Stp1 was found to bind to immunoprecipitated Ira2. Since a catalytically inactive mutant form of Stp1 (Stp1 C11S ) effectively binds to Ira2 without producing any effect on yeast physiology, we conclude that down-regulation of the Ras pathway by Stp1 requires its phosphatase activity. In conclusion, our data suggest a possible cross-talk between tyrosine phosphorylation and the Ras pathway in yeast.

show abstract

“…PDE1 and PDE2 encode the low-and high-affinity cAMP PDEs, respectively, in S. cerevisiae (Sass et al, 1986;Nikawa et al, 1987). Higher sensitivity to heat shock and nutrient starvation has been reported for pde1 and pde2 mutants.…”

Section: Introductionmentioning

confidence: 99%

The cAMP phosphodiesterase encoded by CaPDE2 is required for hyphal development in Candida albicans

Jung

Stateva

2003

Microbiology

View full text Add to dashboard Cite

The cAMP-dependent pathway, which regulates yeast-to-hypha morphogenesis in Candida albicans, is controlled by changes in cAMP levels determined by the processes of synthesis and hydrolysis. Both low-and high-affinity cAMP phosphodiesterases are encoded in the C. albicans genome. CaPDE2, encoding the high-affinity cAMP phosphodiesterase, has been cloned and shown to be toxic in Saccharomyces cerevisiae upon overexpression under pGAL1, but functional under the moderate pMET3. Deletion of CaPDE2 causes elevated cAMP levels and responsiveness to exogenous cAMP, higher sensitivity to heat shock, severe growth defects at 42 6C and highly reduced levels of EFG1 transcription. In vitro in hypha-inducing liquid medium CaPDE2, deletion prohibits normal hyphal, but not pseudohyphal growth. On solid medium capde2 mutants form aberrant hyphae, with fewer branches and almost no lateral buds, which are deficient in hypha-to-yeast reversion. The phenotypic defects of capde2 mutants show that the cAMP-dependent pathway plays specific roles in hyphal and pseudohyphal development, its regulatory role however, being greater in liquid than on solid medium in vitro. The increased expression of CaPDE2 after serum addition correlates well with a drop in cAMP levels following the initial rise in response to the hyphal inducer. These results suggest that Capde2p mediates a desensitization mechanism by lowering basal cAMP levels in response to environmental stimuli in C. albicans.

show abstract

Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae.

Cited by 207 publications

References 40 publications

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

In Saccharomyces cerevisiae an unbalanced level of tyrosine phosphorylation down-regulates the Ras/PKA pathway

The cAMP phosphodiesterase encoded by CaPDE2 is required for hyphal development in Candida albicans

Contact Info

Product

Resources

About