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Tyrosine hydroxylase phosphorylation in digitonin-permeabilized bovine adrenal chromaffin cells: The effects of protein kinase and phosphatase inhibitors on Ser19 and Ser40 phosphorylation



Tyrosine hydroxylase phosphorylation in digitonin-permeabilized bovine adrenal chromaffin cells: The effects of protein kinase and phosphatase inhibitors on Ser19 and Ser40 phosphorylation



Journal of Neurochemistry 69(6): 2387-2396



The protein kinases and protein phosphatases that act on tyrosine hydroxylase in vivo have not been established. Bovine adrenal chromatin cells were permeabilized with digitonin and incubated with (gamma-32P)ATP, in the presence or absence of 10 muM Ca2+, 1muM cyclic AMP, 1 muM phorbol dibutyrate, or various kinase or phosphatase inhibitors. Ca2+ increased the phosphorylation of Ser19 and Ser40. Cyclic AMP, and phorbol dibutyrate in the presence of Ca2+, increased the phosphorylation of only Ser40, Ser31 and Ser8 were not phosphorylated. The Ca2+-stimulated phosphorylation of Ser19 was incompletely reduced by inhibitors of calcium/calmodulin-stimulated protein kinase II (46% with KN93 and 68% with CaM-PKII 273-302), suggesting that another protein kinase(s) was contributing to the phosphorylation of this site. The Ca2+-stimulated phosphorylation of Ser40 was reduced by specific inhibitors of protein kinase A (56% with H89 and 38% with PKAi 5-22 amide) and protein kinase C (70% with Ro 31-8220 and 54% with PKCi 19-31), suggesting that protein kinases A and C contributed to most of the phosphorylation of this site. Results with okadaic acid and microcystin suggested that Ser19 and Ser40 were dephosphorylated by PP2A.

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Accession: 010023129

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PMID: 9375670


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