Protein kinase cAMP-activated catalytic subunit alpha (PKA C-alpha)

Protein kinase cAMP-activated catalytic subunit alpha (PKA C-alpha) is the enzymatic component of protein kinase A responsible for phosphorylation of serine and threonine residues on target proteins, modulated by cellular levels of cyclic AMP (cAMP). Upon cAMP binding to the regulatory subunit, the catalytic subunit is released, becoming active. It plays essential roles in hormonal signaling pathways, energy metabolism, cell cycle regulation, memory formation, and many other cellular functions. Aberrant PKA C-alpha activity has been implicated in the pathogenesis of various cancers, cardiovascular conditions, and endocrine diseases, making it a validated therapeutic and research target[3][7][8][5].

Other names

Protein kinase A catalytic subunit alphacAMP-dependent protein kinase catalytic subunit alphaPKA catalytic subunit alphaPRKACA (gene/protein symbol)

Small molecules/drugs that elevate cAMP (e.g., beta-adrenergic agonists) indirectly activate PKA by increasing cAMP levels, leading to dissociation of the regulatory subunit and activation of the catalytic subunit[2][3][8].