PKA, RII is one of several regulatory subunits of the cAMP-dependent protein kinase (PKA). The kinase holoenzyme consists of two dimmers of two regulatory (R) and two catalytic (C) subunits that dissociate upon the binding of two cAMP molecules to each of the R subunits (1). Two families of R subunits (RI and RII) have been identified, each possessing distinct cAMP binding properties and resulting in different phosphorylation states (2, 3). The PKA, RII beta (RIIb) regulatory isoform is abundant in brown and white adipose tissue and brain, with limited expression elsewhere. PKA, RIIb is demonstrated to play a role in regulating energy balance and adiposity, thus making it a potential target for therapeutic intervention in obesity (4, 5). It has been shown that PKA, RIIb is essential for cAMP-induced growth inhibition and differentiation of HL-60 human leukemia cells. By binding to its ligand, cAMP, the PKA, RIIb cAMP receptor acts as a tumor suppressor protein exerting growth inhibition, differentiation, and reverse transformation (6).
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