• Made available online as an Accepted Preprint 11 February 2010
  • Accepted Preprint first posted online on 11 February 2010

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

  1. Kjetil Taskén
  1. Biotechnology Centre of Oslo and Centre for Molecular Medicine, Nordic EMBL Partnership, University of Oslo, PO Box 1125, Blindern, N-0317 Oslo, Norway
  1. (Correspondence should be addressed to K Taskén; Email: kjetil.tasken{at}biotek.uio.no)


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.

  • Revision received 5 February 2010
  • Accepted 11 February 2010
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