cAMP-dependent protein kinase catalytic subunit beta (PRKACB)

cAMP-dependent protein kinase catalytic subunit beta (PRKACB) is a critical enzyme that serves as one of the catalytic components of the Protein Kinase A (PKA) holoenzyme. It plays a central role in the cAMP signaling pathway, which transduces extracellular signals from various hormones and neurotransmitters into intracellular responses. Upon binding of cAMP to the PKA regulatory subunits, PRKACB is released as an active monomer that phosphorylates a wide array of substrate proteins, thereby regulating processes such as metabolism, gene expression, and cell proliferation. Dysregulation of PRKACB, through mutations or gene fusions, has been implicated in several diseases, including Cushing syndrome, Carney complex, and various cancers such as pancreatobiliary oncocytic neoplasms. In the context of drug development, PRKACB is considered a therapeutic target for its role in oncogenic signaling and endocrine disorders. While specific inhibitors are being explored, the broad biological impact of PKA signaling presents challenges for achieving selectivity and managing potential safety concerns.

Other names

PKA C-betaPKACbProtein kinase cAMP-activated catalytic subunit betaCAFD2Protein kinase cAMP-dependent catalytic beta subunit

ATP-competitive inhibition of kinase activity