ArticleThe Journal of biological chemistry2011
Alterations at dispersed sites cause phosphorylation and activation of SNF1 protein kinase during growth on high glucose.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- A genetic screen reveals a key role for Reg1 in 2-deoxyglucose sensing and yeast AMPK inhibition.PLoS genetics · 2025Article
- 2-deoxyglucose transiently inhibits yeast AMPK signaling and triggers glucose transporter endocytosis, potentiating the drug toxicity.PLoS genetics · 2022Article
- Default Activation and Nuclear Translocation of the Plant Cellular Energy Sensor SnRK1 Regulate Metabolic Stress Responses and Development.The Plant cell · 2019Article
- Feedback Control of Snf1 Protein and Its Phosphorylation Is Necessary for Adaptation to Environmental Stress.The Journal of biological chemistry · 2015Article
- The SNF1 Kinase Ubiquitin-associated Domain Restrains Its Activation, Activity, and the Yeast Life Span.The Journal of biological chemistry · 2015Article
- Network reconstruction and validation of the Snf1/AMPK pathway in baker's yeast based on a comprehensive literature review.NPJ systems biology and applications · 2015Article
- Systematic lipidomic analysis of yeast protein kinase and phosphatase mutants reveals novel insights into regulation of lipid homeostasis.Molecular biology of the cell · 2014Article
- Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae.The Journal of biological chemistry · 2013Article
- Reducing sphingolipid synthesis orchestrates global changes to extend yeast lifespan.Aging cell · 2013Article
- The hybrid four-CBS-domain KINβγ subunit functions as the canonical γ subunit of the plant energy sensor SnRK1.The Plant journal : for cell and molecular biology · 2013Article
- Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation.The Journal of biological chemistry · 2013Article
- Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
The SNF1/AMP-activated protein kinases are central energy regulators in eukaryotes. SNF1 of Saccharomyces cerevisiae is inhibited during growth on high levels of glucose and is activated in response to glucose depletion and other stresses. Activation entails phosphorylation of Thr(210) on the activation loop of the catalytic subunit Snf1 by Snf1-activating kinases. We have used mutational analysis to identify Snf1 residues that are important for regulation. Alteration of Tyr(106) in the αC helix or Leu(198) adjacent to the Asp-Phe-Gly motif on the activation loop relieved glucose inhibition of phosphorylation, resulting in phosphorylation of Thr(210) during growth on high levels of glucose. Substitution of Arg for Gly(53), at the N terminus of the kinase domain, increased activation on both high and low glucose. Alteration of the ubiquitin-associated domain revealed a modest autoinhibitory effect. Previous studies identified alterations of the Gal83 (β) and Snf4 (γ) subunits that relieve glucose inhibition, and we have here identified a distinct set of Gal83 residues that are required. Together, these results indicate that alterations at dispersed sites within each subunit of SNF1 cause phosphorylation of the kinase during growth on high levels of glucose. These findings suggest that the conformation of the SNF1 complex is crucial to maintenance of the inactive state during growth on high glucose and that the default state for SNF1 is one in which Thr(210) is phosphorylated and the kinase is active.
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