Insulin promotes both the phosphorylation and dephosphorylation of proteins in its target cells. Insulin-induced dephosphorylation has long been thought to serve an important regulatory function; the role of insulin-stimulation phosphorylation is less certain. The proteins known to be substrates for this reaction are ATP citrate (pro-3S)-lyase, acetyl-CoA carboxylase, and the ribosomal subunit S6. The evidence as to the physiological role and mechanism underlying the insulin-stimulated phosphorylation of these proteins is summarized. Present information suggests that insulin-stimulated phosphorylation may serve an important regulatory role in certain actions of insulin.
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