Phosphorylation by cyclic AMP‐dependent protein kinase does not affect the association of ATP citrate‐lyase with isolated mitochondria

FEBS Letters

Bridger, William A.¹  Lin, Tianwei¹ 

[1] Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

关键词: ATP citrate-lyase;    Mitochondrion;    cyclic AMP-dependent protein kinase;   

DOI  :  10.1016/0014-5793(87)80477-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

ATP citrate-lyase is known to be a substrate for various protein kinases, but the functional role, if any, of kinase-directed phosphorylation of this enzyme has not been identified. Recently, Strålfors [(1987) J. Biol. Chem. 262, 11486–11489] has suggested that effects on the association of this enzyme with mitochondria may account for the observed ability of isoproteronol or insulin to promote immobilization of ATP citrate-lyase in permeabilized cells. Here we report studies involving phosphorylation of the pure enzyme in vitro using cyclic AMP-dependent protein kinase. We show that phosphorylation has no significant effect on the fraction of the enzyme that may be bound to isolated mitochondria.

【 授权许可】

Unknown