title: Glycolysis controls plasma membrane glucose sensors to promote glucose signaling in yeasts.
abstract: Sensing of extracellular glucose is necessary for cells to adapt to glucose variation in their environment. In the respiratory yeast Kluyveromyces lactis, extracellular glucose controls the expression of major glucose permease gene RAG1 through a cascade similar to the Saccharomyces cerevisiae Snf3/Rgt2/Rgt1 glucose signaling pathway. This regulation depends also on intracellular glucose metabolism since we previously showed that glucose induction of the RAG1 gene is abolished in glycolytic mutants. Here we show that glycolysis regulates RAG1 expression through the K. lactis Rgt1 (KlRgt1) glucose signaling pathway by targeting the localization and probably the stability of Rag4, the single Snf3/Rgt2-type glucose sensor of K. lactis. Additionally, the control exerted by glycolysis on glucose signaling seems to be conserved in S. cerevisiae. This retrocontrol might prevent yeasts from unnecessary glucose transport and intracellular glucose accumulation.
authors.affiliation: Université Lyon 1, CNRS, UMR5240 Microbiologie, Adaptation et Pathogénie, équipe Génétique Moléculaire des Levures, Villeurbanne, France.
authors.forename: Amélie
authors.initials: A
authors.lastname: Cairey-Remonnay
authors.affiliation: Université Lyon 1, CNRS, UMR5240 Microbiologie, Adaptation et Pathogénie, équipe Génétique Moléculaire des Levures, Villeurbanne, France.
authors.forename: Julien
authors.initials: J
authors.lastname: Deffaud
authors.affiliation: Université Lyon 1, CNRS, UMR5240 Microbiologie, Adaptation et Pathogénie, équipe Génétique Moléculaire des Levures, Villeurbanne, France.
authors.forename: Micheline
authors.initials: M
authors.lastname: Wésolowski-Louvel
authors.affiliation: Université Lyon 1, CNRS, UMR5240 Microbiologie, Adaptation et Pathogénie, équipe Génétique Moléculaire des Levures, Villeurbanne, France.
authors.forename: Marc
authors.initials: M
authors.lastname: Lemaire
authors.affiliation: Université Lyon 1, CNRS, UMR5240 Microbiologie, Adaptation et Pathogénie, équipe Génétique Moléculaire des Levures, Villeurbanne, France alexandre.soulard@univ-lyon1.fr.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Soulard
mesh_terms: D001692:Biological Transport; D002462:Cell Membrane; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D025461:Feedback, Physiological; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D005947:Glucose / Q000378:metabolism*; D006019:Glycolysis / Q000235:genetics*; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D007716:Kluyveromyces / Q000235:genetics / Q000378:metabolism*; D009004:Monosaccharide Transport Proteins / Q000235:genetics / Q000378:metabolism; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism
chemical_list: D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D007527:Isoenzymes; D009004:Monosaccharide Transport Proteins; C435343:RAG4 protein, Kluyveromyces; C102114:RGT1 protein, S cerevisiae; C112512:RGT2 protein, S cerevisiae; C104463:SNF3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C031629:phosphoenolpyruvate-glucose phosphotransferase; D005947:Glucose