Protein phosphorylation is quintessential for specific pathways to function. This function can be influenced by internal or external factors. It is a reversible action with the involvement of kinases and phosphatases1. This activity is crucial in the cell cycle, apoptosis, and signal transduction pathways. If a protein is phosphorylated or dephosphorylated when it shouldn’t be, there can be severe disruptions to the cellular pathway. At times, the phosphorylation state can be the cause of a disease. This has been found in degenerative diseases, cancers, and various pathways involving the immune system2. For instance, kinase inhibitors have been successful in cancer treatments.
Enzymes control phosphorylation. Kinases function to add phosphate groups to proteins and phosphatases function to remove phosphates. Typically, phosphorylation occurs on serine, threonine, or tyrosine residues. This process can be very quick or it can take many hours. It results in a conformational change which either activates or inactivates protein activity.