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Insulin receptor substrate proteins are intracellular adaptor proteins that bridge activated insulin and insulin-like growth factor receptors to downstream effectors such as PI3K/Akt and MAPK signaling pathways[8][3][6]. These proteins, particularly IRS-1 and IRS-2, are tyrosine-phosphorylated upon receptor activation, creating docking sites for various signaling molecules[8][3]. IRS proteins regulate glucose uptake, metabolism, cell growth, differentiation, and survival[8][5][4]. Dysregulation or altered expression of IRS proteins has been implicated in insulin resistance and several forms of cancer, making them relevant both as biomarkers and potential therapeutic targets[6][5][8][4].
Drugs can modulate IRS protein phosphorylation (tyrosine/serine/threonine) to restore proper insulin signaling. Some agents downregulate IRS-1/2 expression or activity in cancer contexts to inhibit growth.
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