Details

Autor(en) / Beteiligte

• Halloran, S.M. (University of California, Davis, CA.)
• Vulliet, P.R

Titel

Microtubule-associated protein kinase-2 phosphorylates and activates tyrosine hydroxylase following depolarization of bovine adrenal chromaffin cells

Ist Teil von

• The Journal of biological chemistry, 1994-12, Vol.269 (49), p.30960-30965

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1994

Quelle

MEDLINE

Beschreibungen/Notizen

• Depolarization of cultured bovine adrenal chromaffin cells with KCl increased the activity of a proline-directed protein kinase that phosphorylates tyrosine hydroxylase. Characterization of the KCl-activated protein kinase activity revealed that it shared similar biochemical and chromatographic properties with the microtubule-associated protein-2 kinase/extracellularly regulated kinase (MAP/ERK) family of protein kinases. This protein kinase activity was found to elute from Mono Q, Superose, and phenyl-Sepharose columns under conditions described for MAP/ERK kinases, and active fractions were found to react with specific anti-bodies directed against ERKs. The KCl-activated protein kinase was found to phosphorylate the serine 31 site of endogenous bovine adrenal tyrosine hydroxylase. This phosphorylation resulted in an approximately 2-fold activation of tyrosine hydroxylase