Cyclic AMP-dependent protein kinase catalytic subunit alpha (PKA Cα (also commonly referred to as PRKACA, the gene symbol))

Cyclic AMP-dependent protein kinase catalytic subunit alpha (PKA Cα) is the primary enzymatic component of protein kinase A, a key serine/threonine kinase regulated by cyclic AMP (cAMP)[5][6]. The canonical PKA holoenzyme consists of two regulatory and two catalytic subunits; binding of cAMP to regulatory subunits causes release and activation of the catalytic subunits, which then phosphorylate a broad range of substrates to propagate cAMP-dependent signaling[5][1][3]. PKA Cα plays central roles in regulating metabolism, gene expression, cell cycle, and differentiation, and is essential in mediating the cellular responses to hormones and other signals that stimulate cAMP production[6][1]. Pathogenic mutations or altered expression of PRKACA (which encodes PKA Cα) are associated with several human diseases, including certain cancers and endocrine tumors[6]. Due to its widespread and fundamental role in cell biology, targeted modulation of PKA Cα is primarily of research interest, as therapeutic targeting is challenging and must be approached with caution to avoid significant adverse effects[1][6].

Other names

Protein kinase A catalytic subunit alphaPKA catalytic subunit alphaPRKACA (gene symbol)cAMP-dependent protein kinase catalytic subunit alphaC subunit alpha of PKAPKA Cα

Competitive inhibition of ATP binding site (for kinase inhibitors); Allosteric inhibition of catalytic activity