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Protein kinase cAMP-dependent type II regulatory subunit beta (PRKAR2B) is a regulatory subunit of protein kinase A (PKA), a holoenzyme tetramer involved in cellular signal transduction via cAMP. The inactive PKA holoenzyme consists of two regulatory (R) subunits and two catalytic (C) subunits. Upon cAMP binding, PRKAR2B releases active catalytic subunits, enabling phosphorylation of downstream targets. PRKAR2B is involved in metabolic regulation, immunity, and neuronal signaling, interacts with various anchoring proteins for cellular localization, and modulates transcriptional regulators such as CREB1. Dysregulation or mutation of PRKAR2B is linked to multiple disease states, including cancer and metabolic disorders[2][3][6][7][8].
Drugs/ligands bind to the regulatory subunit and trigger release and activation of catalytic subunits of PKA; Modulation of cAMP binding alters downstream signaling and kinase activity
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