The cyclic adenosine monophosphate (cAMP)-dependent protein kinase regulatory subunit 2 beta (PRKAR2B, also known as A0306) is one of the regulatory subunits of protein kinase A (PKA).
The cyclic adenosine monophosphate (cAMP)-dependent protein kinase regulatory subunit 2 beta (PRKAR2B, also known as A0306) is one of the regulatory subunits of protein kinase A (PKA). PKA belongs to the AGC group of serine/threonine kinases and exists as a tetramer consisting of two regulatory (R) and two catalytic (C) subunits. Four genes encode the R subunits (RIα, RIß, RIIα, and RIIß), and three encode the C subunits (Cα, Cß and Cγ). The enzyme is activated by the binding of cAMP to the R subunits, inducing the dissociation of the interaction between the R and C subunits. The regulatory subunits mediate membrane association by binding to PKA anchoring proteins (AKAPs). This interaction directs kinase localization and substrate specificity. PRKAR2B null mice present disruptions in different metabolic pathways. These mice also show abnormal dendritogenesis, impaired PKA activity, defects in the organization of the cortical layer IV neurons into barrels and decreased phosphorylation of post-synaptic PKA targets, but normal presynaptic phosphorylation. Down-regulation of the PKA RIIβ subunit by antisense oligonucleotides inhibits cAMP-dependent nuclear signaling and cAMP response element binding (CREB) phosphorylation.