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glycogen synthase catalyzes glycogen synthesis. determine whether each of the following are associated with an increase or decrease in glycogen synthase activity.
1) activation of phosphoprotein phosphatase PP1
2) Phosphorylation (inactivation) of phosphoprotein phosphatase 1 (PP1) by PKA
3) Subunit dissociation of cAMP-dependent protein kinase (PKA)
4) Phosphorylation of glycogen synthase
5) Insulin
6) Phosphorylation of glycogen synthase kinase (GSK, or GSK3)
a. Increased glycogen synthase activity:
b. Decreased glycogen synthase activity:

Answer :

At some point, the activity of glycogen synthase increases or decreases increased activity of glycogen synthase. Glycogen synthase kinase phosphorylation (GSK, or GSK3). 

  • Phosphoprotein phosphatase PP1 activation. Insulin Glycogen synthase activity is decreased: Glycogen synthase phosphorylation. PKA phosphorylates (deactivates) the enzyme phosphoprotein phosphatase 1 (PP1). Dissociation of the cAMP-dependent protein kinase's subunit (PKA).
  • Since glucagon and insulin are counter-regulatory hormones, their effects on the degree of glycogen synthase phosphorylation are diametrically opposed. A rise in cAMP and a parallel rise in PKA activity occur as a result of glucagon binding to hepatocyte receptors.
  • At least four distinct locations of glycogen synthase are phosphorylated as a result of PKA. Additionally, PKA activity causes phosphorylase kinase activity on the glycogen synthase to rise at a position where PKA phosphorylates. The activity of cAMP phosphodiesterase, which hydrolyzes AMP and lowers the level of active PKA, is increased by insulin in PKA.

Additionally, insulin inhibits GSK-3 action by reducing the amount of kinase-mediated phosphorylation of glycogen synthase.

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