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REVIEW Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins

Abstract : Protein phosphorylation is the most common post-translational modification observed in cell signaling and is controlled by the balance between protein kinase and phosphatase activities. The cAMP-protein kinase A (PKA) pathway is one of the most studied and well-known signal pathways. To maintain a high level of specificity, the cAMP-PKA pathway is tightly regulated in space and time. A-kinase-anchoring proteins (AKAPs) target PKA to specific substrates and distinct subcellular compartments providing spatial and temporal specificity in the mediation of biological effects controlled by the cAMP-PKA pathway. AKAPs also serve as scaffolding proteins that assemble PKA together with signal terminators such as phosphoprotein phosphatases and cAMP-specific phosphodiesterases as well as components of other signaling pathways into multiprotein-signaling complexes.
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Guillaume Pidoux, Kjetil Taské. REVIEW Specificity and spatial dynamics of protein kinase A signaling organized by A-kinase-anchoring proteins. Journal of Molecular Endocrinology, BioScientifica, 2010, 44 (5), pp.271-284. ⟨10.1677/JME-10-0010⟩. ⟨inserm-02556153⟩

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