ATP-citrate lyase phosphorylation in rat adipose tissue.
1983; Elsevier BV; Volume: 258; Issue: 21 Linguagem: Inglês
10.1016/s0021-9258(17)44056-7
ISSN1083-351X
AutoresDominick Pucci, S. Anantha Ramakrishna, Benjamin Wagner,
Tópico(s)Advanced Proteomics Techniques and Applications
ResumoPrevious in vitro studies demonstrated that ATP-citrate lyase is phosphorylated by cyclic AMP-dependent protein kinase at peptide A, containing a phosphoserine residue, and by ATP-citrate lyase kinase at peptide B, containing both phosphoserine and phosphothreonine residues (Ramakrishna, S., Pucci, D. L., and Benjamin, W. B. (1983) J. Biol. Chem. 258, 4950-4956). In the present study, trypsin-digested, radiolabeled ATP-citrate lyase from rat epididymal fat pads was analyzed by high performance liquid chromatography. Phosphorylation occurred at three amino acid residues within two different peptide sequences; one (peptide a) contained phosphoserine and the other (peptide b) contained phosphoserine and phosphothreonine. The retention times and molecular weights were the same for peptides a and A and peptides b and B. Isoproterenol action increased peptide a phosphorylation and, to a lesser extent, peptide b phosphorylation. Insulin action also increased peptide a phosphorylation, but did not increase peptide b phosphorylation.
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