Glucose-dependent activation of protein kinase A activity in Saccharomyces cerevisiae and phosphorylation of its TPK1 catalytic subunit

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Protein kinase A (PKA), in yeast, plays a major role in controlling metabolism and gene expression in connection with the available nutrient conditions. We here measure, for the first time, a transient change in the in vivo PKA activity, along a cAMP peak produced by 100 mM glucose addition to glyce...

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Detalles Bibliográficos
Autor principal: Portela, P.
Otros Autores: Moreno, S.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2006
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 scopus  |a 2-s2.0-33645106818 
024 7 |2 cas  |a glucose, 50-99-7, 84778-64-3; glycerol, 56-81-5; Cyclic AMP, 60-92-4; Cyclic AMP-Dependent Protein Kinases, EC 2.7.1.37; Glucose, 50-99-7; Glycerol, 56-81-5; kemptide, 65189-71-1; Oligopeptides; Saccharomyces cerevisiae Proteins 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a CESIE 
100 1 |a Portela, P. 
245 1 0 |a Glucose-dependent activation of protein kinase A activity in Saccharomyces cerevisiae and phosphorylation of its TPK1 catalytic subunit 
260 |c 2006 
270 1 0 |m Moreno, S.; Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Pabellón 2, Buenos Aires 1428, Argentina; email: smoreno@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a Protein kinase A (PKA), in yeast, plays a major role in controlling metabolism and gene expression in connection with the available nutrient conditions. We here measure, for the first time, a transient change in the in vivo PKA activity, along a cAMP peak produced by 100 mM glucose addition to glycerol-growing cells as well as a change in the phosphorylation state of its catalytic subunit (Tpk1p) following PKA activation. PKA activity was measured in situ in permeabilized cells, preserving its intracellular localization. Comparison of total PKA activity, measured in situ in permeabilized cells with data obtained from in vitro assays in crude extracts, underscores the inhibitory potency of the regulatory subunit within the cell. Tpk1p phosphorylation was detected through non-denaturing gel electrophoresis. Phosphorylation of Tpk1p increases its specificity constant toward kemptide substrate. The use of mutants of the cAMP pathway showed that phosphorylation depends on the activation of PKA via the G-protein coupled receptor pathway triggered by glucose. The phosphorylation state of Tpk1p was followed during the diauxic shift. Tpk1p phosphorylation is dynamic and reversible: its up-regulation correlates with a fully fermentative metabolism, while its down-regulation with stationary phase or respiratory metabolism. Reversible phosphorylation can thus be considered a new control mechanism possibly pointing to a fine-tuning of PKA activity in response to environmental conditions. © 2005 Elsevier Inc. All rights reserved.  |l eng 
536 |a Detalles de la financiación: Agencia Nacional de Promoción Científica y Tecnológica 
536 |a Detalles de la financiación: Fundación Antorchas 
536 |a Detalles de la financiación: Universidad de Buenos Aires 
536 |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas 
536 |a Detalles de la financiación: We thank S. Rossi for critical revision of the manuscript, P. Valacco for help with written english, and JM Thevelein with help in the provision of several strains. This work was supported by grants from Universidad de Buenos Aires (UBA), CONICET (Consejo Nacional de Investigaciones Científicas y Técnicas), ANPCYT (Agencia Nacional de Promoción Científica y Tecnológica) and Fundación Antorchas. Paula Portela had a fellowship from UBA and from Fundación Antorchas. 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas Y Naturales, Pabellón 2, Buenos Aires 1428, Argentina 
690 1 0 |a CAMP SIGNALLING 
690 1 0 |a GLUCOSE 
690 1 0 |a IN SITU ASSAY 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PKA (PROTEIN KINASE A) 
690 1 0 |a YEAST 
690 1 0 |a CYCLIC AMP DEPENDENT PROTEIN KINASE 
690 1 0 |a G PROTEIN COUPLED RECEPTOR 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCEROL 
690 1 0 |a ANIMAL CELL 
690 1 0 |a ARTICLE 
690 1 0 |a BREATHING 
690 1 0 |a CATALYSIS 
690 1 0 |a CELL MEMBRANE PERMEABILITY 
690 1 0 |a CELL METABOLISM 
690 1 0 |a DOWN REGULATION 
690 1 0 |a EXTRACT 
690 1 0 |a GEL ELECTROPHORESIS 
690 1 0 |a IN VIVO STUDY 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN PHOSPHORYLATION 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a UPREGULATION 
690 1 0 |a CATALYTIC DOMAIN 
690 1 0 |a CYCLIC AMP 
690 1 0 |a CYCLIC AMP-DEPENDENT PROTEIN KINASES 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a GLUCOSE 
690 1 0 |a GLYCEROL 
690 1 0 |a MUTATION 
690 1 0 |a OLIGOPEPTIDES 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a SACCHAROMYCES CEREVISIAE PROTEINS 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a ANIMALIA 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
700 1 |a Moreno, S. 
773 0 |d 2006  |g v. 18  |h pp. 1072-1086  |k n. 7  |p Cell. Signal.  |x 08986568  |w (AR-BaUEN)CENRE-4136  |t Cellular Signalling 
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