The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle.
The ability of insulin to promote the phosphorylation of some proteins and the dephosphorylation of others is paradoxical. An insulin-stimulated protein kinase is shown to activate the type-1 protein phosphatase that controls glycogen metabolism, by phosphorylating its regulatory subunit at a specific serine. Furthermore, the phosphorylation of this residue is stimulated by insulin in vivo. Increased and decreased phosphorylation of proteins by insulin can therefore be explained through the same basic underlying mechanism.
Dent
P
P
Department of Biochemistry, University of Dundee, Scotland, UK.
Lavoinne
A
A
Nakielny
S
S
Caudwell
F B
FB
Watt
P
P
Cohen
P
P
D000595:Amino Acid Sequence; D000818:Animals; D019204:GTP-Binding Proteins / Q000378:metabolism; D006003:Glycogen / Q000096:biosynthesis*; D007328:Insulin / Q000494:pharmacology / Q000502:physiology*; D007700:Kinetics; D008954:Models, Biological; D008969:Molecular Sequence Data; D009132:Muscles / Q000187:drug effects / Q000378:metabolism*; D010766:Phosphorylation; D011433:Propranolol / Q000494:pharmacology; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits
D007328:Insulin; D006003:Glycogen; D011433:Propranolol; D011494:Protein Kinases; D019204:GTP-Binding Proteins