ArticleThe Journal of biological chemistry2012
In vivo phosphorylation of Ser21 and Ser83 during nutrient-induced activation of the yeast protein kinase A (PKA) target trehalase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 75 citations in OpenAlex.
- Article
- Multi-omics profiling reveals the molecular mechanism of Bifidobacterium animalis BB04 in co-culture with Wickerhamomyces anomalus Y-5 to induce bifidocin A synthesis.World journal of microbiology & biotechnology · 2024Article
- Look for the Scaffold: Multifaceted Regulation of Enzyme Activity by 14-3-3 Proteins.Physiological research · 2024Review
- The yeast 14-3-3 proteins Bmh1 and Bmh2 regulate key signaling pathways.Frontiers in molecular biosciences · 2024Review
- Advances inJournal of fungi (Basel, Switzerland) · 2023Review
- Interaction of TOR and PKA Signaling inBiomolecules · 2022Review
- Kveik Brewing Yeasts Demonstrate Wide Flexibility in Beer Fermentation Temperature Tolerance and Exhibit Enhanced Trehalose Accumulation.Frontiers in microbiology · 2022Article
- The involvement of theVirulence · 2021Article
- Genome-Wide Analysis of Nutrient Signaling Pathways Conserved in Arbuscular Mycorrhizal Fungi.Microorganisms · 2021Article
- A novel yeast hybrid modeling framework integrating Boolean and enzyme-constrained networks enables exploration of the interplay between signaling and metabolism.PLoS computational biology · 2021Article
- The trehalose-6-phosphate phosphatase Tps2 regulatesAutophagy · 2021Article
- Regulation of trehalase activity by multi-site phosphorylation and 14-3-3 interaction.Scientific reports · 2021Article
- Nutrient sensing and cAMP signaling in yeast: G-protein coupled receptor versus transceptor activation of PKA.Microbial cell (Graz, Austria) · 2020Article
- Phosphoproteome Response to Dithiothreitol Reveals UniqueJournal of proteome research · 2020Article
- A protein kinase A-regulated network encodes short- and long-lived cellular memories.Science signaling · 2020Article
- Chemical Genetics of AGC-kinases Reveals Shared Targets of Ypk1, Protein Kinase A and Sch9.Molecular & cellular proteomics : MCP · 2020Article
- 14-3-3 Proteins: a window for a deeper understanding of fungal metabolism and development.World journal of microbiology & biotechnology · 2019Review
- PKA and HOG signaling contribute separable roles to anaerobic xylose fermentation in yeast engineered for biofuel production.PloS one · 2019Article
- A Snapshot of the Trehalose Pathway During Seed Imbibition inFrontiers in plant science · 2019Article
- Function of TFIIIC, RNA polymerase III initiation factor, in activation and repression of tRNA gene transcription.Nucleic acids research · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The readdition of an essential nutrient to starved, fermenting cells of the yeast Saccharomyces cerevisiae triggers rapid activation of the protein kinase A (PKA) pathway. Trehalase is activated 5-10-fold within minutes and has been used as a convenient reporter for rapid activation of PKA in vivo. Although trehalase can be phosphorylated and activated by PKA in vitro, demonstration of phosphorylation during nutrient activation in vivo has been lacking. We now show, using phosphospecific antibodies, that glucose and nitrogen activation of trehalase in vivo is associated with phosphorylation of Ser(21) and Ser(83). Unexpectedly, mutants with reduced PKA activity show constitutive phosphorylation despite reduced trehalase activation. The same phenotype was observed upon deletion of the catalytic subunits of yeast protein phosphatase 2A, suggesting that lower PKA activity causes reduced trehalase dephosphorylation. Hence, phosphorylation of trehalase in vivo is not sufficient for activation. Deletion of the inhibitor Dcs1 causes constitutive trehalase activation and phosphorylation. It also enhances binding of trehalase to the 14-3-3 proteins Bmh1 and Bmh2, suggesting that Dcs1 inhibits by preventing 14-3-3 binding. Deletion of Bmh1 and Bmh2 eliminates both trehalase activation and phosphorylation. Our results reveal that trehalase activation in vivo is associated with phosphorylation of typical PKA sites and thus establish the enzyme as a reliable read-out for nutrient activation of PKA in vivo.
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