The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle
P Dent, A Lavoinne, S Nakielny, FB Caudwell, P Watt… - Nature, 1990 - nature.com
Nature, 1990•nature.com
The ability of insulin to promote the phosphoryl-ation 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 …
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 …
Abstract
The ability of insulin to promote the phosphoryl-ation 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.
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