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. 2015 Oct 1;6:203. doi: 10.3389/fphar.2015.00203

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Copyright © 2015 Boularan and Gales.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Schematic structure of PKA and EPAC. (A) The catalytic (c) subunit of cAMP-dependent Protein Kinase (PKA) is a serine/threonine protein kinase associated, in the absence of cAMP, with the regulatory (R) subunit to form the inactive PKA holoenzyme. cAMP can bind to A or B sites in the regulatory subunits and induces the dissociation of the catalytic subunits. (B) Epac structure showing the conserved cAMP binding domain (CBD), Disheveled/Egl-10/pleckstrin (DEP) domain, RAS exchange motif (REM) domain, RAS association (RA) domain, and CDC25-homology domain (CDC25HD).