Abstract
Synaptosomal proteins isolated from rat cerebral cortex were phosphorylated endogeneously in the presence of [γ- 32P]ATP. The phosphorylated proteins were found to be membrane bound by differential and density gradient centrifugation. In contrast to the phosphorylation of all synaptosomal proteins, phosphorylation of one protein (C), 41 000–43 000 daltons, was inhibited by Mg 2+ and stimulated by Ca 2+. In addition, the ionophores X537A and A23187, as well as papaverine, selectively enhanced phosphorylation of protein C without affecting phosphorylation of the other proteins. Cyclic AMP did not influence the phosphorylation of protein C but markedly affected the phosphorylation of other synaptosomal proteins. It appears that the phosphorylation of protein C is stimulated by agents which trigger the release of neurotransmitters (Ca 2+, X537A, A23187 and papaverine), and is inhibited by Mg 2+, which inhibits release. It is proposed that the phosphorylation of protein C is related to membranal events underlying the release of neurotransmitters.
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