cAMP-dependent protein kinase type II-alpha regulatory subunit (PRKAR2A)

cAMP-dependent protein kinase type II-alpha regulatory subunit (PRKAR2A) is a regulatory component of the cAMP-dependent protein kinase (Protein Kinase A, PKA) holoenzyme. PRKAR2A binds cAMP, controlling the activation of PKA by facilitating the release of its catalytic subunits upon cAMP binding. This regulatory subunit is phosphorylated by the catalytic subunit and interacts with A-kinase anchoring proteins (AKAPs), impacting the localization and specificity of PKA signaling in various subcellular compartments. PRKAR2A is broadly expressed, with prominent roles in the intestine, heart, liver, and lungs. It is implicated in cellular functions such as signal transduction, cell metabolism, intracellular protein transport, and inflammation. Disruption of PRKAR2A function has been linked to diseases including cancer (e.g., fibrolamellar carcinoma), Carney complex, and inflammatory disorders, with preclinical evidence suggesting modulation of PRKAR2A influences disease severity in inflammatory bowel disease models[1][2][3][5][7].

Other names

PRKAR2APKR2PRKAR2cAMP-dependent protein kinase regulatory subunit RII alphaprotein kinase A RII-alpha subunitprotein kinase cAMP-dependent type II regulatory subunit alphaprotein kinase, cAMP-dependent, regulatory subunit type II alphacAMP-dependent protein kinase type II-alpha regulatory subunit

Modulation of PKA activity via competitive binding to catalytic subunits\nChanges in cellular cAMP signaling dynamics\nIndirect modulation through altering phosphorylation state of cellular targets