Protein Kinase, cAMP Dependent Catalytic Beta (PRKACb)

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.

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