In eukaryotes, nutrient availability and metabolism are coordinated by sensing mechanisms and signaling pathways, which influence a broad set of cellular functions such as transcription and metabolic pathways to match environmental conditions. In yeast, PKA is activated in the presence of high glucose concentrations, favoring fast nutrient utilization, shutting down stress responses, and boosting growth.Onthe contrary, Snf1/AMPK is activated in the presence of low glucose or alternative carbon sources, thus promoting an energy saving program through transcriptional activation and phosphorylation of metabolic enzymes. The PKA and Snf1/AMPK pathways share common downstream targets. Moreover, PKA has been reported to negatively influence the activation of Snf1/AMPK. We report a new cross-talk mechanism with a Snf1-dependent regulation of the PKA pathway. We show that Snf1 and adenylate cyclase (Cyr1) interact in a nutrient-independent manner. Moreover, we identify Cyr1 as a Snf1 substrate and show that Snf1 activation state influences Cyr1 phosphorylation pattern, cAMP intracellular levels, and PKA-dependent transcription.

Nicastro, R., Tripodi, F., Gaggini, M., Castoldi, A., Reghellin, V., Nonnis, S., et al. (2015). Snf1 phosphorylates adenylate cyclase and negatively regulates protein kinase A-dependent transcription in Saccharomyces cerevisiae. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 290(41), 24715-24726 [10.1074/jbc.M115.658005].

Snf1 phosphorylates adenylate cyclase and negatively regulates protein kinase A-dependent transcription in Saccharomyces cerevisiae

NICASTRO, RAFFAELE
Primo
;
TRIPODI, FARIDA
Secondo
;
REGHELLIN, VERONICA;COCCETTI, PAOLA
Ultimo
2015

Abstract

In eukaryotes, nutrient availability and metabolism are coordinated by sensing mechanisms and signaling pathways, which influence a broad set of cellular functions such as transcription and metabolic pathways to match environmental conditions. In yeast, PKA is activated in the presence of high glucose concentrations, favoring fast nutrient utilization, shutting down stress responses, and boosting growth.Onthe contrary, Snf1/AMPK is activated in the presence of low glucose or alternative carbon sources, thus promoting an energy saving program through transcriptional activation and phosphorylation of metabolic enzymes. The PKA and Snf1/AMPK pathways share common downstream targets. Moreover, PKA has been reported to negatively influence the activation of Snf1/AMPK. We report a new cross-talk mechanism with a Snf1-dependent regulation of the PKA pathway. We show that Snf1 and adenylate cyclase (Cyr1) interact in a nutrient-independent manner. Moreover, we identify Cyr1 as a Snf1 substrate and show that Snf1 activation state influences Cyr1 phosphorylation pattern, cAMP intracellular levels, and PKA-dependent transcription.
Articolo in rivista - Articolo scientifico
AMP-activated kinase (AMPK); Cyr1; adenylate cyclase (adenylyl cyclase); cyclic AMP (cAMP); protein kinase A (PKA); yeast; AMP-Activated Protein Kinases; Biocatalysis; Cyclic AMP-Dependent Protein Kinases; Enzyme Activation; Gene Expression Regulation, Fungal; Glucose; Mitochondrial Proteins; Mutation; Phenotype; Phosphorylation; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription, Genetic; Biochemistry; Cell Biology; Molecular Biology
English
2015
290
41
24715
24726
partially_open
Nicastro, R., Tripodi, F., Gaggini, M., Castoldi, A., Reghellin, V., Nonnis, S., et al. (2015). Snf1 phosphorylates adenylate cyclase and negatively regulates protein kinase A-dependent transcription in Saccharomyces cerevisiae. THE JOURNAL OF BIOLOGICAL CHEMISTRY, 290(41), 24715-24726 [10.1074/jbc.M115.658005].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/138740
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