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Literature summary for 2.4.1.11 extracted from
- Dysregulation of glycogen synthase COOH- and NH2-terminal phosphorylation by insulin in obesity and type 2 diabetes mellitus (2009), J. Clin. Endocrinol. Metab., 94, 4547-4556.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | glycogen synthase activity correlates inversely with phosphorylation of glycogen synthase sites 2 + 2a and 3a. Insulin significantly decreases 2 + 2a phosphorylation in lean subjects only and induces a larger dephosphorylation at site 3 in lean compared with obese subjects. The exaggerated insulin resistance in type 2 diabetes mellitus compared with obese subjects is not reflected by differences in site 3 phosphorylation but is accompanied by a significantly higher site 1b phosphorylation during insulin stimulation. Hyperphosphorylation of another Ca2/calmodulin-dependent kinase-II target, phospholamban-Thr17, is also evident in type 2 diabetes mellitus. Dephosphorylation of glycogen synthase by phosphatase treatment fully restores glycogen synthase activity in all groups | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
patients with obesity and type 2 diabetes mellitus | - |
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Release 2023.1 (January 2023)
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