Proteins interacting with protein kinase A from Saccharomyces cerevisiae

ROSSI, SILVIA.; GALELLO FIORELLA; GONZALEZ BARDECI NICOLAS; MORENO SILVIA

Potrero de los Funes- San Luis

Congreso; 47 Reunion Anual de la SAIB; 2011

SAIB

Subcellular targeting through the association with adaptor and scaffolding proteins has emerged as a key mechanism in signaling specificity. Compartmentalization of cAMP-PKA pathway is maintained by A kinase anchoring proteins (AKAPs) which interact with PKA regulatory subunit (R). PKA AKAPs in mammals are classified in RII, RI or dual specificity. In S.cerevisiae the anchoring of PKA is poorly understood. We have identified proteins that tether the R subunit (Bcy1) from yeast PKA, in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although of PKA is poorly understood. We have identified proteins that tether the R subunit (Bcy1) from yeast PKA, in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although of PKA is poorly understood. We have identified proteins that tether the R subunit (Bcy1) from yeast PKA, in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although of PKA is poorly understood. We have identified proteins that tether the R subunit (Bcy1) from yeast PKA, in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although S.cerevisiae the anchoring of PKA is poorly understood. We have identified proteins that tether the R subunit (Bcy1) from yeast PKA, in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although characterization of the Bcy1-binding domains showed that although in vitro and in vivo. The characterization of the Bcy1-binding domains showed that although a-helices were predicted, they do not show the characteristics of the amphipathic helix of PKA AKAPs. The key residues for the interaction are positively charged residues. These characteristics are shared with RISR (RI Specifier Region) present in dual specificity AKAPs. The amino termini of R subunits constitute the so called D/D domain, responsible for its dimerization and its interaction with anchoring proteins. Chemical crosslinking experiments confirm that Bcy1 exists as a dimer, via its N-terminus. The N-terminus of Bcy1 is necessary for the interaction with the tethering proteins of yeast PKA. The modelling by homology of the N-terminus of Bcy1 shows that it shares with its counterparts the residues important for dimerization but that the exposed surface has characteristics of its own. amphipathic helix of PKA AKAPs. The key residues for the interaction are positively charged residues. These characteristics are shared with RISR (RI Specifier Region) present in dual specificity AKAPs. The amino termini of R subunits constitute the so called D/D domain, responsible for its dimerization and its interaction with anchoring proteins. Chemical crosslinking experiments confirm that Bcy1 exists as a dimer, via its N-terminus. The N-terminus of Bcy1 is necessary for the interaction with the tethering proteins of yeast PKA. The modelling by homology of the N-terminus of Bcy1 shows that it shares with its counterparts the residues important for dimerization but that the exposed surface has characteristics of its own. amphipathic helix of PKA AKAPs. The key residues for the interaction are positively charged residues. These characteristics are shared with RISR (RI Specifier Region) present in dual specificity AKAPs. The amino termini of R subunits constitute the so called D/D domain, responsible for its dimerization and its interaction with anchoring proteins. Chemical crosslinking experiments confirm that Bcy1 exists as a dimer, via its N-terminus. The N-terminus of Bcy1 is necessary for the interaction with the tethering proteins of yeast PKA. The modelling by homology of the N-terminus of Bcy1 shows that it shares with its counterparts the residues important for dimerization but that the exposed surface has characteristics of its own. amphipathic helix of PKA AKAPs. The key residues for the interaction are positively charged residues. These characteristics are shared with RISR (RI Specifier Region) present in dual specificity AKAPs. The amino termini of R subunits constitute the so called D/D domain, responsible for its dimerization and its interaction with anchoring proteins. Chemical crosslinking experiments confirm that Bcy1 exists as a dimer, via its N-terminus. The N-terminus of Bcy1 is necessary for the interaction with the tethering proteins of yeast PKA. The modelling by homology of the N-terminus of Bcy1 shows that it shares with its counterparts the residues important for dimerization but that the exposed surface has characteristics of its own. -helices were predicted, they do not show the characteristics of the amphipathic helix of PKA AKAPs. The key residues for the interaction are positively charged residues. These characteristics are shared with RISR (RI Specifier Region) present in dual specificity AKAPs. The amino termini of R subunits constitute the so called D/D domain, responsible for its dimerization and its interaction with anchoring proteins. Chemical crosslinking experiments confirm that Bcy1 exists as a dimer, via its N-terminus. The N-terminus of Bcy1 is necessary for the interaction with the tethering proteins of yeast PKA. The modelling by homology of the N-terminus of Bcy1 shows that it shares with its counterparts the residues important for dimerization but that the exposed surface has characteristics of its own.