Herrera R, Rosen O M
J Recept Res. 1987;7(1-4):405-15. doi: 10.3109/10799898709054995.
The insulin receptor is a hormone-dependent protein tyrosine kinase that belongs to the family of tyrosine kinases associated with growth factor receptors and oncogene products. The activity of the insulin receptor kinase is regulated by the phosphorylation state of specific domains of the protein. Phosphorylation of the receptor on tyrosine residues activates its kinase activity whereas phosphorylation on serine and/or threonine residues inhibits it. In this review, we discuss the evidence that supports a role of the kinase activity of the receptor in the molecular mechanism of insulin action.
胰岛素受体是一种激素依赖性蛋白酪氨酸激酶，属于与生长因子受体和癌基因产物相关的酪氨酸激酶家族。胰岛素受体激酶的活性受该蛋白特定结构域磷酸化状态的调节。受体酪氨酸残基的磷酸化激活其激酶活性，而丝氨酸和/或苏氨酸残基的磷酸化则抑制该活性。在本综述中，我们讨论了支持受体激酶活性在胰岛素作用分子机制中发挥作用的证据。
