The
Insulin-like Growth Factor 1 (IGF-1) Receptor is a
transmembrane receptor that is activated by
IGF-1 and by the related growth factor
IGF-2. It belongs to the large class of
tyrosine kinase receptors. This receptor mediates the effects of IGF-1, which is a polypeptide protein hormone similar in molecular structure to insulin. IGF-1 plays an important role in growth and continues to have anabolic effects in adults - meaning that it can induce hypertrophy of
skeletal muscle and other target tissues. Mice lacking the IGF-1 receptor die late in development, and show a dramatic reduction in body mass, testifying to the strong growth-promoting effect of this receptor. Mice carrying only one functional copy of igf1r are normal, but exhibit a ~15% decrease in body mass.
Structure
Two alpha subunits and two beta subunits make up the
IGF-1 receptor. Both the α and β subunits are synthesized from a single mRNA precursor. The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane αβ chain. The α chains are located extracellularly while the β subunit spans the membrane and are responsible for intracellular signal transduction upon ligand stimulation. The mature IGF-IR has a molecular weight of approximately 320 kDa. The receptor is a member of a family which consists of the
Insulin Receptor and the
IGF-2R (and their respective ligands IGF-1 and IGF-2),...
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