Lin T W, Bridger W A
Department of Biochemistry, University of Alberta, Edmonton, Canada.
FEBS Lett. 1987 Nov 30;224(2):322-4. doi: 10.1016/0014-5793(87)80477-5.
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.
已知ATP柠檬酸裂解酶是多种蛋白激酶的底物，但这种酶的激酶导向磷酸化的功能作用（如果有的话）尚未确定。最近，斯特拉尔福斯[（1987年）《生物化学杂志》262卷，11486 - 11489页]提出，对这种酶与线粒体结合的影响可能解释了异丙肾上腺素或胰岛素促进ATP柠檬酸裂解酶在通透细胞中固定的观察到的能力。在此，我们报告了使用环磷酸腺苷依赖性蛋白激酶在体外对纯酶进行磷酸化的研究。我们表明，磷酸化对可能与分离的线粒体结合的酶的比例没有显著影响。
