In liver cells, the activity of PFK-1 is regulated by the PFK-2/FBP-2 complex, whose activity is in turn controlled by glucagon and insulin.
Glucagon activates protein kinase A. Then protein kinase A phosphorylates the PFK-2/FBP-2 complex, so that the PFK-2/FBP-2 complex will make fructose-6P from fructose-2,6-bisP. Since fructose-2,6-bisP activates PFK-1 (in liver cells), without it the process of glycolysis will slow down.
However I read from my notes that protein kinase A is dependent on cAMP (so that when the energy level is low, the increase in cAMP will cause protein kinase A to increase in activity). It seems that protein kinase A should help increase glycolysis, so why does activating it by glucagon cause glycolysis to slow down instead?