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

  • Lin T
  • Bridger W
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Abstract

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. © 1987.

Author-supplied keywords

  • ATP citrate-lyase
  • Mitochondrion
  • cyclic AMP-dependent protein kinase

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Authors

  • Tianwei Lin

  • William A. Bridger

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