Insulin Dependent Tyrosine Protein Kinase (also known as Insulin Receptor Tyrosine Kinase or Insulin Receptor) is a protein kinase enzyme that plays a crucial role in insulin signaling pathways and glucose metabolism within the human body.
Insulin is a hormone that regulates blood sugar levels, and its effects are mediated through the insulin receptor. The insulin receptor is a transmembrane protein located on the cell surface of various tissues, including fat, muscle, and liver cells. It consists of two extracellular α-subunits and two intracellular β-subunits. The β-subunits possess tyrosine kinase activity.
When released by the pancreas in response to elevated blood glucose levels, insulin binds to the extracellular α-subunits of the receptor. This binding promotes a conformational change, resulting in the activation of the tyrosine kinase activity of the β-subunits.
Once activated, the receptor phosphorylates specific tyrosine residues on target proteins, including insulin receptor substrate (IRS) proteins, leading to their recruitment and subsequent activation of downstream signaling pathways. These pathways regulate various cellular processes, such as glucose uptake, glycogen synthesis, protein synthesis, and lipid metabolism.
Insufficient or defective insulin signaling, such as in insulin resistant or diabetic individuals, can lead to dysregulated blood glucose levels and contribute to the development of metabolic disorders, such as type 2 diabetes. Therefore, understanding the function and regulation of Insulin Dependent Tyrosine Protein Kinase is crucial for studying insulin resistance and developing therapeutic interventions for diabetes.
