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Title: Novel mechanisms in nutrient activation of the yeast protein kinase A pathway
Authors: Thevelein, Johan ×
Bonini, Beatriz Monge
Castermans, Dries
Haesendonckx, Steven
Kriel, Johan
Louwet, Wendy
Thayumanavan, Palvannan
Popova, Yulia
Rubio-Texeira, Marta
Schepers, Wim
Vandormael, Patrick
Van Zeebroeck, Griet
Verhaert, Peter
Versele, Matthias
Voordeckers, Karin #
Issue Date: Jun-2008
Publisher: Akademiai Kiado
Series Title: Acta Microbiologica et Immunologica Hungarica vol:55 issue:2 pages:75-89
Abstract: In yeast the Protein Kinase A (PKA) pathway can be activated by a variety of nutrients. Fermentable sugars, like glucose and sucrose, trigger a spike in the cAMP level, followed by activation of PKA and phosphorylation of target proteins causing a.o. mobilization of reserve carbohydrates, repression of stress-related genes and induction of growth-related genes. Glucose and sucrose are sensed by a G-protein coupled receptor system that activates adenylate cyclase and also activates a bypass pathway causing direct activation of PKA. Addition of other essential nutrients, like nitrogen sources or phosphate, to glucose-repressed nitrogen- or phosphate-starved cells, also triggers rapid activation of the PKA pathway. In these cases cAMP is not involved as a second messenger. Amino acids are sensed by the Gap1 transceptor, previously considered only as an amino acid transporter. Recent results indicate that the amino acid ligand has to induce a specific conformational change for signaling. The same amino acid binding site is involved in transport and signaling. Similar results have been obtained for Pho84 which acts as a transceptor for phosphate activation of the PKA pathway. Ammonium activation of the PKA pathway in nitrogen-starved cells is mediated mainly by the Mep2 transceptor, which belongs to a different class of transporter proteins. Hence, different types of sensing systems are involved in control of the yeast PKA pathway by nutrients.
URI: 
ISSN: 1217-8950
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Microbiology and Biotechnology Section - miscellaneous
Laboratory for Molecular Cell Biology (-)
× corresponding author
# (joint) last author

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