title: ATP-citrate lyase kinase and cyclic AMP-dependent protein kinase phosphorylate different sites on ATP-citrate lyase.
abstract: ATP-citrate lyase was phosphorylated by highly purified cyclic AMP-independent protein kinase (ATP-citrate lyase kinase) or the catalytic subunit of cyclic AMP-dependent protein kinase. Each kinase phosphorylated ATP-citrate lyase equally but the combination of both kinases increased ATP-citrate lyase phosphorylation additively. When ATP-citrate lyase was phosphorylated with each kinase and partially digested with either L-1-tosylamido-2-phenylmethyl chloromethyl ketone-treated trypsin or Staphylococcus aureus protease followed by electrophoresis of the proteolytic products on sodium dodecyl sulfate-polyacrylamide gels or when the phosphorylated lyase was completely digested by these proteases followed by chromatography and electrophoresis, the results showed that the site phosphorylated by ATP-citrate lyase kinase was different from that phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase. Only phosphoserine was found in lyase phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase whereas phosphoserine and phosphothreonine were found in ATP-citrate lyase phosphorylated by lyase kinase.
mesh_terms: D001275:ATP Citrate (pro-S)-Lyase / Q000378:metabolism*; D000273:Adipose Tissue / Q000201:enzymology; D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation; D011485:Protein Binding; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits; D051381:Rats
chemical_list: D010446:Peptide Fragments; D000242:Cyclic AMP; D001275:ATP Citrate (pro-S)-Lyase; D011494:Protein Kinases; C032202:ATP-citrate lyase kinase