Insulin receptor (INSR) (INSR)

The Insulin receptor (INSR) is a transmembrane receptor tyrosine kinase essential for maintaining glucose homeostasis and regulating metabolic processes (UniProt P06213). Upon binding insulin, the receptor undergoes autophosphorylation of its intracellular tyrosine residues, which triggers the recruitment and activation of insulin receptor substrates (IRS-1/2) and downstream signaling through the PI3K/Akt and MAPK pathways (PubMed: 21864752). These pathways stimulate glucose uptake in peripheral tissues like muscle and fat while suppressing hepatic glucose production (StatPearls: Insulin Resistance). Mutations in the INSR gene are directly linked to severe insulin resistance syndromes, such as Donohue syndrome and Rabson-Mendenhall syndrome, and play a significant role in the pathogenesis of Type 2 diabetes (NIH: MedlinePlus Genetics). Therapeutic management involves the use of exogenous insulin analogs that bind and activate the receptor to lower blood glucose levels, though this carries risks such as hypoglycemia and weight gain (PubChem: Insulin).

Other names

INSRIRCD220Insulin receptor subunit alphaInsulin receptor subunit betaHHF5

Binding of insulin to the extracellular alpha subunits of the receptor induces a conformational change that activates the intrinsic tyrosine kinase activity of the intracellular beta subunits, leading to autophosphorylation and the recruitment of adapter proteins to initiate metabolic and mitogenic signaling cascades.