Protein kinase cAMP-dependent type I regulatory subunit beta (PRKAR1B)

Protein kinase cAMP-dependent type I regulatory subunit beta (PRKAR1B) is a key regulatory subunit of the PKA holoenzyme, which mediates cellular responses to cAMP. The PKA holoenzyme consists of two regulatory subunits (including PRKAR1B as RIβ) and two catalytic subunits. Upon cAMP binding, the complex dissociates, allowing the catalytic subunits to phosphorylate diverse protein targets. PRKAR1B is most highly expressed in the nervous system, especially cerebral cortex and hypothalamus, and its dysfunction causes neurodevelopmental disorders and contributes to tumorigenesis in some contexts. It serves as a cAMP receptor within the cell and anchors the PKA complex to specific subcellular locations via AKAP proteins, modulating key processes such as metabolism, ion transport, transcription, and neuronal signaling

Other names

PRKAR1BProtein kinase cAMP-dependent type I regulatory subunit betacAMP-dependent protein kinase type I-beta regulatory subunitProtein kinase, cAMP-dependent, regulatory subunit type I betaProtein kinase, cAMP-dependent, regulatory, type I, betaPRKAR1MASNSRIβprotein kinase cAMP-dependent type 1 regulatory subunit beta

Drugs that **modulate PKA activity** (by influencing cAMP levels, such as agonists of Gs-coupled GPCRs, PDE inhibitors, or adenylyl cyclase activators) indirectly affect PRKAR1B function as part of the PKA holoenzyme