Insulin is a small peptide hormone released by the beta cells of the pancreas following a meal rich in carbohydrates.

When we
ingest the carbohydrates, these macromolecules are subsequently broken down into their glucose monomers. This increases
the concentration of glucose in the blood. Since high levels of glucose in the blood can be toxic to the body, the cells of our
body such as skeletal muscle cells absorb the glucose and store it in the form of glycogen. Insulin is the primary messenger of
the signal transduction pathway that allows the cells to uptake glucose and transform it into glycogen. Insulin binds onto the
insulin receptor, which itself contains tyrosine protein kinase domains. Upon the binding of insulin, these tyrosine kinase
domains undergo cross-phosphorylation that induces a confirmation change and activates the receptor. The receptor then
binds an insulin-receptor substrate (IRS) molecule, which is a protein that acts as an adaptor and attaches another molecule
called phosphoinositide 3-kinase. This kinase phosphorylates a PIP2 into a PIP3, which then moves on and attaches to PIP3-
dependent protein kinase (PDK). PDK in turn activates protein kinase B (also called Akt), which is able to diffuse across the
cytoplasm and activate the formation of glycogen from glucose and stimulate the transfer of glucose transporters onto the
membrane for the uptake of extracellular glucose molecules.