Functional regulation of reconstituted Na, K‐ATPase by protein kinase A phosphorylation

FEBS Letters

Logvinenko, Ninel¹  Cornelius, Flemming² 

[1] Department of Paediatrics, St. Göran's Cildren's Hospital, Karolinska Institutet, S-112 81 Lund, Sweden;Department of Biophysics, University of Aarhus, DK-8000 Aarhus C, Denmark

关键词: Protein kinase A (PKA);    Regulation;    Na+;    K+-ATPase;    Reconstitution;    Phosphorylation;   

DOI  :  10.1016/0014-5793(96)00032-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Reconstituted Na⁺,K⁺-ATPase from either pig kidney or shark rectal glands was phosphorylated by cAMP dependent protein kinase, PKA. The stoichiometry was ∼ 0.9 mole P_i/mole α-subunit in the pig kidney enzyme and ∼ 0.2 mol P_i/mol α-subunit in the shark enzyme. In shark Na⁺,K⁺-ATPase PKA phosphorylation increased the maximum hydrolytic activity for cytoplasmic Na⁺ activation and extracellular K⁺ activation without affecting the apparent K _m values. In contrast, no significant functional effect after PKA phosphorylation was observed in pig kidney Na⁺,K⁺-ATPase.

【 授权许可】

Unknown