Casein Kinase 2 Alpha 2 (CSNK2a2)

Casein kinase II catalyzes the phosphorylation of serine or threonine residues in proteins; i.e., it is a protein serine / threonine kinase. The enzyme is probably present in all eukaryotic cells, implying that it has fundamental cellular functions. The holoenzyme is a tetramer containing 2 alpha or alpha-prime subunits (or one of each) and 2 beta subunits. The function of the beta subunit is unknown but presumably it fills a regulatory role in the holoenzyme. The alpha subunit is the catalytic subunit. Angiotensin II, a potent inducer of cardiomyocyte hypertrophy, induced proteasomal degradation of p27 in primary rat cardiomyocytes through CK2-alpha-prime-dependent phosphorylation of p27 on ser83 and thr187, which are conserved in human and rodents. Conversely, unphosphorylated p27 potently inhibited CK2-alpha-prime.