Insulin signal transduction pathway is secreted after glucose enters the beta cell and that triggers several other processes in a chain reaction. While insulin is secreted by the pancreas to lower blood glucose levels, glucagon is secreted to raise blood glucose levels. This is why glucagon has been known for decades as a counter-regulatory hormone. When blood glucose levels are low, the pancreas secretes glucagon, which in turn causes the liver to convert stored glycogen polymers into glucose monomers, which is then released into the blood. This process is called glycogenolysis. Liver cells, or hepatocytes, have glucagon receptors which allow for glucagon to attach
Insulin known as a homodimer. Insulin binds to the α-subunits of the homodimer, which faces the extracellular side of the cells. The β subunits have tyrosine kinase enzyme activity which is triggered by the insulin binding. This activity provokes the autophosphorylation of the β subunits and subsequently the phosphorylation of proteins inside the cell known as insulin receptor substrates (IRS). The phosphorylation of the IRS activates a signal transduction cascade that leads to the activation of other kinases as well as transcription factors that mediate the intracellular effects of insulin. The cascade that leads to the insertion of GLUT4 glucose transporters