Proximity Ligation Analysis of protein-protein interactions between MAP3K3 and PRKACA. HeLa cells were stained with anti-MAP3K3 rabbit purified polyclonal 1:1200 and anti-PRKACA mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex, and nuclei were counterstained with DAPI (blue).
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme 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 have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of cAMP-dependent protein kinase. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq
PKA C-alpha,cAMP-dependent protein kinase catalytic subunit alpha,cAMP-dependent protein kinase catalytic subunit alpha, isoform 1,protein kinase A catalytic subunit