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Glycogen synthase kinase 3β interaction protein functions as an A-kinase anchoring protein

Item Type:Article
Title:Glycogen synthase kinase 3β interaction protein functions as an A-kinase anchoring protein
Creators Name:Hundsrucker, C., Skroblin, P., Christian, F., Zenn, M., Popara, V., Joshi, M., Eichhorst, J., Wiesner, B., Herberg, F.W., Reif, B., Rosenthal, W. and Klussmann, E.
Abstract:A-kinase anchoring proteins (AKAPs) include a family of scaffolding proteins that target protein kinase A (PKA) and other signaling proteins to cellular compartments and thereby confine the activities of the associated proteins to distinct regions within cells. AKAPs bind PKA directly. The interaction is mediated by the dimerization and docking domain of regulatory subunits of PKA and the PKA-binding domain of AKAPs. Analysis of the interactions between the dimerization and docking domain and various PKA-binding domains yielded a generalized motif allowing the identification of AKAPs. Our bioinformatics and peptide array screening approaches based on this signature motif identified GSKIP (glycogen synthase kinase 3beta interaction protein) as an AKAP. GSKIP directly interacts with PKA and GSK3beta (glycogen synthase kinase 3beta). It is widely expressed and facilitates phosphorylation and thus inactivation of GSK3beta by PKA. GSKIP contains the evolutionarily conserved domain of unknown function 727. We show here that this domain of GSKIP and its vertebrate orthologues binds both PKA and GSK3beta and thereby provides a mechanism for the integration of PKA and GSK3beta signaling pathways.
Keywords:Evolution/Protein, Phosphorylation/Kinases/Serine-Threonine, Protein/Protein-Protein Interactions, Signal Transduction/Adapter Proteins, Signal Transduction/Cyclic Nucleotides/Cyclic AMP, Signal Transduction/Protein Kinases, Signal Transduction/Protein Kinases/Cyclic Nucleotide, Signal Transduction/Protein Kinases/Serine/Threonine, Glycogen Synthase Kinase 3, AKAP
Source:Journal of Biological Chemistry
Publisher:American Society for Biochemistry and Molecular Biology
Page Range:5507-5521
Date:19 February 2010
Official Publication:https://doi.org/10.1074/jbc.M109.047944
PubMed:View item in PubMed

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