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. 1991 Oct 15;180(1):191-6.
doi: 10.1016/s0006-291x(05)81275-6.

Phosphorylation and functional modification of calmodulin-dependent protein kinase IV by cAMP-dependent protein kinase

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Phosphorylation and functional modification of calmodulin-dependent protein kinase IV by cAMP-dependent protein kinase

I Kameshita et al. Biochem Biophys Res Commun. .

Abstract

Calmodulin-dependent protein kinase IV (CaM-kinase IV), a neuronal calmodulin-dependent multifunctional protein kinase, undergoes autophosphorylation in response to Ca2+ and calmodulin, resulting in activation of the enzyme (Frangakis et al. (1991) J. Biol. Chem. 266, 11309-11316). In contrast, the enzyme was phosphorylated by cAMP-dependent protein kinase, leading to a decrease in the enzyme activity. Thus, the results suggest differential regulation of CaM-kinase IV by two representative second messengers, Ca2+ and cAMP.

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