cAMP induces dissociation of inactive PKA tetramers Authored: Le Novere, N, Jassal, B, 2004-03-31 12:22:05 Edited: Jassal, B, 2008-11-06 10:17:49 Pubmed16407073 Reactome Database ID Release 43111925 Reactome, http://www.reactome.org ReactomeREACT_1532 Reviewed: Castagnoli, L, 2008-11-06 12:55:54 The four protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The specific isoform activated in response to glucagon signalling is not known. The PKA kinase is a tetramer of two regulatory and two catalytic. The regulatory subunits block the catalytic subunits. Binding of cAMP to the regulatory subunit leads to the dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit. has a Stoichiometric coefficient of 2 has a Stoichiometric coefficient of 4 PKA tetramer PKA catalytic subunit cAMP:PKA regulatory subunit