Human GYS1 (Glycogen synthase 1) knockout HeLa cell lysate

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Glycogen synthase 1 (GYS1) also known as muscle glycogen synthase catalyzes the synthesis of glycogen from glucose. It adds glucose units from UDP-glucose to the non-reducing ends of glycogen chains facilitating glycogen elongation. The molecular mass of GYS1 is approximately 85 kDa. It is predominantly expressed in skeletal muscle tissue providing energy storage primarily in the form of glycogen. GYS1 is regulated through phosphorylation wherein it undergoes inactive to active conformational changes.

Biological function summary

This enzyme plays a critical role in the energy storage mechanism of muscle tissues. GYS1 functions as a part of the glycogen synthase complex interacting with various glycogen-associated proteins to modulate its activity. These interactions control the enzyme's affinity for its substrate and its susceptibility to regulatory signals like phosphorylation affecting glycogen synthesis efficiency. Through its activity GYS1 ensures a readily available reserve of glucose in muscle tissues for rapid energy production when required.

Pathways

Glycogen synthase 1 is a central component of the glycogen metabolism pathway. It acts alongside other enzymes such as glycogen phosphorylase which catalyzes glycogen breakdown. The balance between GYS1 and glycogen phosphorylase determines the rate of glycogen turnover within cells. GYS1 is further regulated by the insulin signaling pathway where insulin promotes glycogen synthesis by altering GYS1 activity alongside proteins like AKT influencing glucose homeostasis and energy management in tissues.

Associated diseases and disorders

Dysregulation of GYS1 activity often associates with glycogen storage diseases notably Type 0 where deficiencies in glycogen storage lead to episodes of low blood sugar and reduced exercise capacity. Furthermore aberrations in GYS1 function contribute to insulin resistance and Type 2 diabetes conditions linked with impaired glucose metabolism. Altered GYS1 activity impacts proteins like glycogen phosphorylase affecting overall glycogen metabolism balance and contributing to metabolic disorders.