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

Journal

JOURNAL OF MOLECULAR ENDOCRINOLOGY
Volume 44, Issue 5, Pages 271-284

Publisher

BIOSCIENTIFICA LTD
DOI: 10.1677/JME-10-0010

Keywords

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Funding

  1. Functional Genomics Program
  2. Research Council of Norway
  3. The Norwegian Cancer Society
  4. Novo Nordic Research Foundation

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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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