The binding of insulin to its receptor activates a protein tyrosine kinase that

Question

The binding of insulin to its receptor activates a protein tyrosine kinase that transfers phosphate groups to tyrosine residues on the opposite b subunit of the receptor and to [____] molecules, which themselves bind to and activate downstream effectors, leading to increased glucose uptake, [____], and protein synthesis. In adult-onset diabetes, in which the cells show a resistance to insulin, it has been thought that the disease was due to a defect in [____] function. Now it appears that the defect may be due to a(n) [____] phosphatase required to remove the initial activation phosphorylation of the receptor, leading to an inactive and unresponsive receptor complex.

(1) insulin receptor substrate; glycogen synthesis; receptor; overactive

(2) MAP kinase; glycogen breakdown; insulin receptor; inactive

(3) insulin receptor substrate; glycogen synthesis; insulin synthesis; defective

(4) IRS; glycogen breakdown; insulin; missing

(5) glycogen; RNA synthesis; insulin receptor; inactive

Explanation / Answer

The binding of insulin to its receptor activates a protein tyrosine kinase that transfers phosphate groups to tyrosine residues on the opposite b subunit of the receptor and to insulin receptor substrate molecules, which themselves bind to and activate downstream effectors, leading to increased glucose uptake,glycogen synthesis, and protein synthesis. In adult-onset diabetes, in which the cells show a resistance to insulin, it has been thought that the disease was due to a defect in receptor function. Now it appears that the defect may be due to a(n) overactive phosphatase required to remove the initial activation phosphorylation of the receptor, leading to an inactive and unresponsive receptor complex.

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