Enhanced amino acid utilization sustains growth of cells lacking Snf1/AMPK

Biochim Biophys Acta. 2015 Jul;1853(7):1615-25. doi: 10.1016/j.bbamcr.2015.03.014. Epub 2015 Apr 2.


The metabolism of proliferating cells shows common features even in evolutionary distant organisms such as mammals and yeasts, for example the requirement for anabolic processes under tight control of signaling pathways. Analysis of the rewiring of metabolism, which occurs following the dysregulation of signaling pathways, provides new knowledge about the mechanisms underlying cell proliferation. The key energy regulator in yeast Snf1 and its mammalian ortholog AMPK have earlier been shown to have similar functions at glucose limited conditions and here we show that they also have analogies when grown with glucose excess. We show that loss of Snf1 in cells growing in 2% glucose induces an extensive transcriptional reprogramming, enhances glycolytic activity, fatty acid accumulation and reliance on amino acid utilization for growth. Strikingly, we demonstrate that Snf1/AMPK-deficient cells remodel their metabolism fueling mitochondria and show glucose and amino acids addiction, a typical hallmark of cancer cells.

Keywords: Budding yeast; Gene chip; Glucose; Metabolism; Respiration; Saccharomyces cerevisiae.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases / deficiency*
  • AMP-Activated Protein Kinases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acids / metabolism*
  • Biocatalysis / drug effects
  • Carbon / metabolism
  • Cell Proliferation
  • Cellular Reprogramming / drug effects
  • Citric Acid Cycle / drug effects
  • Fatty Acids / biosynthesis
  • Fermentation / drug effects
  • Gene Deletion
  • Gene Expression Regulation, Fungal / drug effects
  • Genes, Fungal
  • Glucose / pharmacology
  • Glutamic Acid / metabolism
  • Glycolysis / drug effects
  • Glycolysis / genetics
  • Models, Biological
  • Oxidative Phosphorylation / drug effects
  • Protein Serine-Threonine Kinases / deficiency
  • Protein Serine-Threonine Kinases / metabolism
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Transcription, Genetic / drug effects
  • Up-Regulation / drug effects


  • Amino Acids
  • Fatty Acids
  • Glutamic Acid
  • Carbon
  • Adenosine Triphosphate
  • SNF1-related protein kinases
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Glucose