Role of insulin-stimulated protein phosphorylation in insulin action.
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.
D001275:ATP Citrate (pro-S)-Lyase / Q000378:metabolism*; D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000502:physiology; D002147:Calmodulin / Q000502:physiology; D000242:Cyclic AMP / Q000502:physiology; D007328:Insulin / Q000502:physiology*; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins / Q000378:metabolism*
D002147:Calmodulin; D007328:Insulin; D038601:Ribosomal Protein S6; D012269:Ribosomal Proteins; D000242:Cyclic AMP; D001275:ATP Citrate (pro-S)-Lyase; D011494:Protein Kinases; D008025:Ligases; D000103:Acetyl-CoA Carboxylase; D002118:Calcium