Abstract: The multifunctional calmodulin‐dependent protein kinase (calmodulin‐kinase) from rat brain was autophosphorylated in a Ca2+‐and calmodulin‐dependent manner. The activity of the autophosphorylated enzyme was independent of Ca2+ and calmodulin. Calmodulin‐kinase was dephosphorylated by protein phosphatase C from bovine brain, which is the catalytic subunits of protein phosphatases 1 and 2A. The holoenzyme of protein phosphatase 2A was also involved in the dephosphorylation of the enzyme. The autophosphorylated sites of calmodulin‐kinase were universally dephosphorylated by protein phosphatase C. Calmodulin‐kinase was inactivated and reactivated by autophosphorylation and dephosphorylation, respectively. Furthermore, the regulation of calmodulin‐kinase by autophosphorylation and dephosphorylation was observed using calmodulin‐kinase from canine heart. These results suggest that the activity of calmodulin‐kinase is regulated by autophosphorylation and dephosphorylation, and that the regulation is the universal phenomenon for many other calmodulin‐kinases in various tissues.
|Number of pages||7|
|Journal||Journal of Neurochemistry|
|Publication status||Published - 1987 Oct|
- Ca/calmodulin‐dependent protein kinase
- Protein phosphatase C
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience