Phosphorylation by cyclic AMP-dependent protein kinase does not affect the association of ATP citrate-lyase with isolated mitochondria.
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.
Lin
T W
TW
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Bridger
W A
WA
D001275:ATP Citrate (pro-S)-Lyase / Q000378:metabolism*; D000818:Animals; D002451:Cell Compartmentation; D000242:Cyclic AMP / Q000378:metabolism; D066298:In Vitro Techniques; D008928:Mitochondria / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats
D010750:Phosphoproteins; D000242:Cyclic AMP; D001275:ATP Citrate (pro-S)-Lyase; D011494:Protein Kinases