In molecular biology, the insulin receptor is a transmembrane receptor that is activated by insulin. It belongs to the large class of tyrosine kinase receptors.

Two alpha subunits and two beta subunits make up the insulin receptor. The beta subunits pass through the cellular membrane and are linked by disulfide bonds.

Tyrosine kinase receptors, including, the insulin receptor, mediate their activity by causing the addition of a phosphate groups to particular tyrosines on certain proteins within a cell. The "substrate" proteins which are phosphorylated by the Insulin Receptor include a protein called "IRS1" for "insulin receptor substrate 1". IRS1 binding and phosphorylation eventually leads to an increase in glucose transporter (Glut4) molecules on the outer membrane of insulin-responsive tissues, including muscle cells, liver and adipose tissue, and therefore to an increase in the uptake of glucose from blood into these tissues. Briefly, the glucose transporter (Glut4), is transported from cellular vesicles to the cell surface, where it then can mediate the transport of glucose into the cell.

Thus the main activity of activation of the insulin receptor is inducing glucose uptake. For this reason "insulin insensitvity", or a decrease in insulin receptor signaling, leads to Type II Diabetes - the cells are unable to take up glucose, and the result is hyperglycemia (an increase in circulating glucose), and all the sequelae which result from diabetes.

A few patients with homozygous mutations in the INSR gene have been described which causes Donohue Syndrome or Leprechaunism. In most cases the outlook for these patients is poor with death occurring in the first year of life.

See also

• Insulin
• Insulin resistance

External links

• OMIM entry ^*

Biology | Biochemistry | Tyrosine kinase receptors | Receptors

Receptor de insulina