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Title: Nutrient sensing systems for rapid activation of the protein kinase A pathway in yeast
Authors: Thevelein, Johan ×
Geladé, Ruud
Holsbeeks, Inge
Lagatie, Ole
Popova, Yulia
Rolland, Filip
Stolz, Frank
Van de Velde, Sam
Van Dijck, Patrick
Vandormael, Patrick
Van Nuland, An
Van Roey, Kim
Van Zeebroeck, Griet
Yan, Bing #
Issue Date: Jan-2005
Publisher: Portland Press
Series Title: Biochemical Society Transactions vol:33 issue:Pt 1 pages:253-6
Abstract: The cAMP-protein kinase A (PKA) pathway in the yeast Saccharomyces cerevisiae controls a variety of properties that depend on the nutrient composition of the medium. High activity of the pathway occurs in the presence of rapidly fermented sugars like glucose or sucrose, but only as long as growth is maintained. Growth arrest of fermenting cells or growth on a respiratory carbon source, like glycerol or ethanol, is associated with low activity of the PKA pathway. We have studied how different nutrients trigger rapid activation of the pathway. Glucose and sucrose activate cAMP synthesis through a G-protein-coupled receptor system, consisting of the GPCR Gpr1, the Galpha protein Gpa2 and its RGS protein Rgs2. Glucose is also sensed intracellularly through its phosphorylation. Specific mutations in Gpr1 abolish glucose but not sucrose signalling. Activation of the PKA pathway by addition of a nitrogen source or phosphate to nitrogen- or phosphate-starved cells, respectively, is not mediated by an increase in cAMP. Activation by amino acids is triggered by the general amino acid permease Gap1, which functions as a transporter/receptor. Short truncation of the C-terminus results in constitutively activating alleles. Activation by ammonium uses the ammonium permeases Mep1 and Mep2 as receptor. Specific point mutations in Mep2 uncouple signalling from transport. Activation by phosphate is triggered a.o. by the Pho84 phosphate permease. Several mutations in Pho84 separating transport and signalling or triggering constitutive activation have been obtained.
URI: 
ISSN: 0300-5127
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Microbiology and Biotechnology Section - miscellaneous
Department of Materials Engineering - miscellaneous
Laboratory for Molecular Cell Biology (-)
Materials Technology TC, Campus Group T Leuven
Technologiecluster Materialentechnologie
× corresponding author
# (joint) last author

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