Insulin R/CD220 Products

Description

Biological actions of insulin and IGF1 are mediated by their respective cell surface receptors, both of which are receptor tyrosine kinases that regulate multiple signaling pathways through activation of a series of phosphorylation cascades. The Insulin Receptor and IGF1R are heterotetrameric proteins consisting of two ligand-binding alpha subunits and two beta subunits that each contain a tyrosine kinase domain. Insulin/IGF1 binding to the extracellular domain leads to autophosphorylation of the receptor and activation of the intrinsic tyrosine kinase activity, which allows appropriate substrates to be phosphorylated. These two receptors differ in sequence in regions that confer specificity for the designated ligand as well as in certain intracellular signaling domains. These differences allow insulin and IGF-1 to regulate different physiological functions through receptors that share a very similar structure. Phosphorylation sites that are unique to each receptor presumably play a key role in these signaling differences. The catalytic loops within the tyrosine kinase domains of the IR/IGF1R contain a three tyrosine motif corresponding to Tyr1158, 1162 and 1163 (for the Insulin Receptor) and Tyr1131, 1135 and 1136 (for the IGF1R). It is generally believed that autophosphorylation within the activation loop proceeds in a processive manner initiating at the second tyrosine (1162 or 1135), followed by phosphorylation at the first tyrosine (1158 or 1131), then the last (1163 or 1136), upon which the Insulin Receptor or IGF1R becomes fully active.

Bioinformatics

Entrez	3643 Human
Product By Gene ID	3643
Alternate Names	CD 220 CD220 antigen CD220 EC 2.7.10 EC 2.7.10.1 HHF5 INSR Insulin R insulin receptor InsulinR IR

Research Areas for Insulin R/CD220

Find related products by research area and learn more about each of the different research areas below.

Lipid and Metabolism
Neuroscience
Phospho-Specific
Protein Kinase
Signal Transduction
Tyrosine Kinases