Autophosphorylation of calmodulin-dependent protein kinase IV from rat cerebral cortex.

Calmodulin-dependent protein kinase IV from rat cerebral cortex undergoes autophosphorylation in response to Ca2+ and calmodulin, resulting in its marked enzymatic activation. Autophosphorylation occurred at several sites on CaM-kinase IV, depending upon the enzyme concentration. Among them, Ser437 was almost exclusively phosphorylated at enzyme concentrations lower than 10 micrograms/ml, and autophosphorylation at Ser437 was responsible for marked activation of the enzyme through decreases in the Km values for its substrates and an increase in the Vmax value. The Ca2+/calmodulin-independent activity of CaM-kinase IV was also markedly stimulated by autophosphorylation, but even after autophosphorylation it amounted only about 17% of the total enzyme activity detected in the presence of Ca2+/calmodulin.