The activation loop of PKA catalytic isoforms is differentially phosphorylated by Pkh protein kinases in Saccharomyces cerevisiae

PDK1 (phosphoinositide-dependent protein kinase 1) phosphorylates and activates PKA (cAMP-dependent protein kinase) in vitro. Docking of the HM (hydrophobic motif) in the C-terminal tail of the PKA catalytic subunits on to the PIF (PDK1-interacting fragment) pocket of PDK1 is a critical step in this...

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Autor principal: Haesendonckx, S.
Otros Autores: Tudisca, V., Voordeckers, K., Moreno, S., Thevelein, J.M, Portela, P.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2012
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Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-84870021524 
024 7 |2 cas  |a glutathione transferase, 50812-37-8; Cyclic AMP-Dependent Protein Kinase Catalytic Subunits, 2.7.11.11; Cyclic AMP-Dependent Protein Kinase Type I, 2.7.11.11; Cyclic AMP-Dependent Protein Kinases, 2.7.11.11; Isoenzymes; PKH1 protein, S cerevisiae, 2.7.11.1; Protein-Serine-Threonine Kinases, 2.7.11.1; Saccharomyces cerevisiae Proteins; TPK2 protein, S cerevisiae, 2.7.1.-; Tpk3 protein, S cerevisiae, 2.7.11.11 
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030 |a BIJOA 
100 1 |a Haesendonckx, S. 
245 1 4 |a The activation loop of PKA catalytic isoforms is differentially phosphorylated by Pkh protein kinases in Saccharomyces cerevisiae 
260 |c 2012 
270 1 0 |m Portela, P.; Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Buenos Aires 1428, Argentina; email: pportela@qb.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a PDK1 (phosphoinositide-dependent protein kinase 1) phosphorylates and activates PKA (cAMP-dependent protein kinase) in vitro. Docking of the HM (hydrophobic motif) in the C-terminal tail of the PKA catalytic subunits on to the PIF (PDK1-interacting fragment) pocket of PDK1 is a critical step in this activation process. However, PDK1 regulation of PKA in vivo remains controversial. Saccharomyces cerevisiae contains three PKA catalytic subunits, TPK1, TPK2 and TPK3. We demonstrate that Pkh [PKB (protein kinase B)-activating kinase homologue] protein kinases phosphorylate the activation loop of each Tpk in vivo with various efficiencies. Pkh inactivation reduces the interaction of each catalytic subunit with the regulatory subunit Bcy1 without affecting the specific kinase activity of PKA. Comparative analysis of the in vitro interaction and phosphorylation of Tpks by Pkh1 shows that Tpk1 and Tpk2 interact with Pkh1 through an HM-PIF pocket interaction. Unlike Tpk1, mutagenesis of the activation loop site in Tpk2 does not abolish in vitro phosphorylation, suggesting that Tpk2 contains other, as yet uncharacterized, Pkh1 target sites. Tpk3 is poorly phosphorylated on its activation loop site, and this is due to the weak interaction of Tpk3 with Pkh1 because of the atypical HM found in Tpk3. In conclusion, the results of the present study show that Pkh protein kinases contribute to the divergent regulation of the Tpk catalytic subunits. © The Authors Journal compilation © 2012 Biochemical Society.  |l eng 
593 |a Department of Molecular Biology, University of Geneva, CH-1211, Switzerland 
593 |a Laboratory of Molecular Cell Biology, Institute of Botany and Microbiology, KU Leuven, Kasteelpark Arenberg 31, B-3001 Leuven-Heverlee, Flanders, Belgium 
593 |a Department of Molecular Microbiology, VIB, Leuven-Heverlee, Flanders, Belgium 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Pabellón 2, Buenos Aires 1428, Argentina 
593 |a VIB Laboratory for Systems Biology, Gaston Geenslaan 1, B-3001 Leuven, Belgium 
690 1 0 |a BCY1 
690 1 0 |a CAMP-DEPENDENT PROTEIN KINASE (PKA) 
690 1 0 |a PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1 (PDK1) 
690 1 0 |a PKB (PROTEIN KINASE B)-ACTIVATING KINASE HOMOLOGUE (PKH) 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a TPK 
690 1 0 |a CYCLIC AMP DEPENDENT PROTEIN KINASE 
690 1 0 |a FUNGAL ENZYME 
690 1 0 |a GLUTATHIONE TRANSFERASE 
690 1 0 |a HYBRID PROTEIN 
690 1 0 |a PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1 
690 1 0 |a PROTEIN KINASE B ACTIVATING KINASE HOMOLOGUE 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ARTICLE 
690 1 0 |a CATALYSIS 
690 1 0 |a CULTURE MEDIUM 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a ENZYME ACTIVE SITE 
690 1 0 |a ENZYME ASSAY 
690 1 0 |a ENZYME PHOSPHORYLATION 
690 1 0 |a ENZYME PURIFICATION 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a FUNGUS CULTURE 
690 1 0 |a FUNGUS GROWTH 
690 1 0 |a IN VITRO STUDY 
690 1 0 |a IN VIVO STUDY 
690 1 0 |a NONHUMAN 
690 1 0 |a PLASMID 
690 1 0 |a POLYACRYLAMIDE GEL ELECTROPHORESIS 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN PROTEIN INTERACTION 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a WESTERN BLOTTING 
690 1 0 |a YEAST 
690 1 0 |a AMINO ACID MOTIFS 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a CATALYTIC DOMAIN 
690 1 0 |a CYCLIC AMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNITS 
690 1 0 |a CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE I 
690 1 0 |a CYCLIC AMP-DEPENDENT PROTEIN KINASES 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a ISOENZYMES 
690 1 0 |a MOLECULAR SEQUENCE DATA 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a PROTEIN-SERINE-THREONINE KINASES 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
690 1 0 |a SACCHAROMYCES CEREVISIAE PROTEINS 
690 1 0 |a SACCHAROMYCES CEREVISIAE 
650 1 7 |2 spines  |a MUTAGENESIS 
700 1 |a Tudisca, V. 
700 1 |a Voordeckers, K. 
700 1 |a Moreno, S. 
700 1 |a Thevelein, J.M. 
700 1 |a Portela, P. 
773 0 |d 2012  |g v. 448  |h pp. 307-320  |k n. 3  |p Biochem. J.  |x 02646021  |w (AR-BaUEN)CENRE-205  |t Biochemical Journal 
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