Differential phosphorylation of ribosomal protein S6 in isolated rat hepatocytes after incubation with insulin and glucagon

Richard E H Wettenhall, Philip Cohen, Barry Caudwell, Ross Holland

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    Glucagon and insulin both stimulated the 32P-labelling of ribosomal protein S6 in rat hepatocytes that had been incubated with 32Pi. Glucagon selectively enhanced the labelling of the tryptic peptide phosphorylated by cyclic AMP-dependent protein kinase, demonstrating that 6 S is a physiological substrate for this enzyme. Insulin stimulated the phosphorylation of distinct tryptic peptides, at least one of which appears to be very close in the primary structure to the sites phosphorylated by cyclic AMP-dependent protein kinase.

    Original languageEnglish
    Pages (from-to)207-213
    Number of pages7
    JournalFEBS Letters
    Issue number2
    Publication statusPublished - 8 Nov 1982



    • Cyclic AMP
    • Glucagon
    • Hepatocytes
    • Insulin
    • Protein synthesis
    • Ribosomes

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