Insulin Receptor Takes Center Stage

The defining characteristic of diabetes is its failure to properly maintain blood glucose levels. Normally, the elevated glucose concentration that occurs after eating induces the release of the hormone insulin from pancreatic beta cells. Cells expressing the insulin receptor can bind insulin and respond to the signal, thereby maintaining glucose homeostasis through changes in gene expression patterns and cellular metabolism. Insulin-induced effects include enhanced glucose uptake and glycogen s

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During the American Diabetes Association national conference this year in Philadelphia, scientists gathered to discuss recent advances in this field at a session on positive and negative elements in signal transduction. When all was said and done, some puzzle pieces were added, but questions remain.

Because diabetes essentially results from the body's failure to respond to insulin, some researchers are trying to understand the signal transduction pathways that translate the binding of insulin to its receptor into cellular activity changes. The insulin receptor's cytoplasmic portion contains an inherent tyrosine kinase activity that becomes active on extracellular insulin binding, leading to the receptor's autophosphorylation and transphosphorylation of the insulin receptor substrates (IRS-1-3).1 These proteins associate with the regulatory subunit of phosphoinositol-3-kinase (PI3K), activating the enzyme's catalytic subunit, which adds a phosphate group to the 3'-OH position of the inositol ring in inositol phospholipids.

The reaction's products activate 3'-phosphoinositide-dependent kinase (PDK1), which ...

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