The phosphorylation of choline acetyltransferase

Neurochemical Research
G Bruce, L B Hersh

Abstract

Human placental Choline Acetyltransferase (ChAT) has been shown to be phosphorylated in vitro by kinases present in rat brain. Phosphorylation occurs at a single site with the exclusive phosphoamino acid being serine. ChAT phosphorylation was shown to be calcium, and not cyclic nucleotide, dependent and was inhibited by inhibitors of calcium/calmodulin protein kinases including anti-calmodulin anti-sera. ChAT phosphorylation was stimulated by calmodulin (9 fold) and, to a lesser extent, by phosphatidylserine (4 fold). These results indicate the involvement of a calcium/calmodulin and possibly also a calcium/phospholipid kinase. This finding was confirmed by demonstrating ChAT phosphorylation using both purified multifunctional calcium/calmodulin protein kinase (CaMK) and calcium/phospholipid protein kinase C (PKC) from rat brain. A stoichiometric incorporation of 0.9 mol phosphate/mol ChAT was achieved by CaMK. Phosphorylated ChAT could be isolated from freshly prepared rat brain synaptosomes. The results obtained with this model system support the hypothesis that in vivo a fraction of ChAT exists phosphorylated.

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Citations

Jan 1, 1993·Progress in Biophysics and Molecular Biology·S Tucek
Dec 1, 1992·Neurochemistry International·C Tanaka, N Saito
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Dec 18, 2002·The Journal of Biological Chemistry·Tomas DobranskyR Jane Rylett
May 1, 1994·Journal of Neurochemistry·D Wu, L B Hersh

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