The role of AKAP12 in coordination of VEGF-induced endothelial cell motility


  • R. Walker-Gray
  • E. Klussmann


  • Acta Physiologica


  • Acta Physiol 228 (1): e13359


  • In this issue of Acta Physiologica, Benz et al. study the role of one important protein in the cyclic AMP signaling pathway, the A-kinase anchoring (AKAP)12. The downstream effects stemming from cAMP release are tightly controlled and activate a profusion of signaling pathways. However, many of these different processes function with largely the same major constituent proteins, including adenylate cyclases, kinases, phosphatases, and phosphodiesterases. cAMP-dependent protein kinase (PKA), which is the main intracellular target for cAMP, is widely found in these signaling assemblies, and is present at high concentrations in many tissues, playing varied roles in the regulation of molecular processes. Unexpectedly, despite its ubiquity there are only four isoforms of PKA regulatory subunit with which to impart functional and locational specificity.