The in vitro phosphorylation of actin from rat cerebral cortex

Abstract
Actin was phosphorylated by a cyclic AMP-stimulated protein kinase in a lysed synaptosomal fraction incubated with [γ-32P]ATP, while calcium had no effect on endogenous labeling of the protein. Incubation of an intact synaptosomal fraction with32P-inorganic phosphate did not lead to any detectable phosphorylation of actin in the presence or absence of dibutryl-cyclic AMP, or chemical depolarization. It is suggested that actin is not phosphorylated in the physiologically relevant intact synaptosomes but gains access to protein kinases on lysis.

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