IRS1 is the substrate for the insulin tyrosine kinase receptor and is found in a variety of insulin-responsive cells and tissues. IRS1 protein has no intrinsic enzymatic activity but acts as a docking protein, via the SH2 domains, for mediating the insulin downstream signaling events. IRS1 has been shown to associate with the 14-3-3 family of proteins and this could play a role in the regulation of insulin sensitivity by interrupting the association between the insulin receptor and IRS1. IRS1 may be associated with colorectal cancer and diet and related factors may affect the risk by modifying plasma insulin levels. Thus, the inter-individual variation in insulin signaling mediated by IRS1 may play a plausible role in the development of colorectal cancer.
The Journal of biological chemistry, 272(40), 25267-25274 (1997-10-06)
Insulin binding to its receptor induces the phosphorylation of cytosolic substrates, insulin receptor substrate (IRS)-1 and IRS-2, which associate with several Src homology-2 domain-containing proteins. To identify unique IRS-1-binding proteins, we screened a human heart cDNA library with 32P-labeled recombinant
Breast cancer research and treatment, 104(2), 197-209 (2006-10-20)
An insulin-related pathway to breast cancer has been hypothesized. We examine the 19 CA repeat of the IGF1 gene, the -202 C > A IGFBP3, the G972R IRS, and the G1057D IRS2 polymorphisms among 1,175 non-Hispanic white (NHW) and 576
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