학술논문

Snf1 Phosphorylates Adenylate Cyclase and Negatively Regulates Protein Kinase A-dependent Transcription in Saccharomyces cerevisiae.
Document Type
Article
Source
Journal of Biological Chemistry. 10/9/2015, Vol. 290 Issue 41, p24715-24726. 12p.
Subject
*ADENYLATE cyclase
*CYCLIC-AMP-dependent protein kinase
*GENETIC transcription
*SACCHAROMYCES cerevisiae
*EUKARYOTES
*CELLULAR control mechanisms
*PHOSPHORYLATION
*FUNGI
Language
ISSN
0021-9258
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. On the 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. [ABSTRACT FROM AUTHOR]