Protein Kinase, cAMP Dependent Catalytic Alpha (PRKACa)

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the AMP-activated protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans.

PRKACais a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK. Alternatively spliced transcript variants encoding distinct isoforms have been observed.