Provoked changes in cellular calcium controlled protein phosphorylation and activity of quinate:NAD+ oxidoreductase in carrot cells

FEBS Letters

Ranjeva, Raoul¹  Boudet, Alain M.¹  Graziana, Annick¹ 

[1] Centre de Physiologie Végétale (L.A. CNRS no.241), Université Paul Sabatier 118, route de Narbonne, 31062 Toulouse Cédex, France

关键词: Calcium;    A-23187 Ionophore;    Calmodulin;    Protein phosphorylation;    Protein kinase;    (Carrot);   

DOI  :  10.1016/0014-5793(83)80522-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Quinate:NAD⁺ oxidoreductase activity decreased when carrot cell-suspension cultures were supplemented with the Ca²⁺-ionophore, A-23187 and EGTA. The protein phosphorylation pattern changed as judged by autoradiography. The loss in enzyme activity was correlated with the Ca²⁺ efflux. Addition of Ca²⁺ to protein extracts in combination with calmodulin or not had no effect. Initial quinate:NAD⁺ oxidoreductase activity was partially recovered only after preincubation with ATP-Mg²⁺ and Ca²⁺. The reactivation was abolished by EGTA or fluphenazine. It is concluded that cellular Ca²⁺ controls the enzyme activity by affecting its degree of phosphorylation in vivo.

【 授权许可】

Unknown