Insulin receptor substrates (IRS), the major intracellular substrates of the insulin receptor (IR), are adaptor proteins that transduce signals from the IR to downstream effectors that are important for the biological effect of insulin (1, 2). After insulin stimulation, IRS proteins are rapidly phosphorylated on multiple tyrosine residues. Once phosphorylated, IRS proteins bind and activate Grb-2, SHP2 and the PI3-K p85 subunit (2, 3). IRS-1 functions as one of the key regulators of IR and the insulin-like growth factor-1 receptor. Disruption of IRS-1 causes growth retardation and insulin resistance associated with hypertension, hypertriglyceridemia, and impaired endothelium-dependent vascular relaxation (4, 5).
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