Zick Y
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Crit Rev Biochem Mol Biol. 1989;24(3):217-69. doi: 10.3109/10409238909082554.
Promising progress in understanding the molecular basis of insulin action has been achieved by demonstrating that the insulin receptor is an insulin-sensitive tyrosine kinase. Here we discuss the structure of this receptor kinase and compare it with receptors for related growth factors. We review the known modes to regulate the receptor kinase activity, either through its autophosphorylation (on tyrosine residues) or through its phosphorylation by other kinases (on serine and threonine residues). We discuss the role of the receptor kinase activity in hormone signal transduction in light of results indicating a reduced kinase activity in insulin-resistant states. Finally, studies to identify natural substrates for the insulin receptor kinase are presented. The possible physiological role of these phosphorylated substrates in mediating insulin action is evaluated.
通过证明胰岛素受体是一种对胰岛素敏感的酪氨酸激酶，在理解胰岛素作用的分子基础方面已取得了有前景的进展。在此，我们讨论这种受体激酶的结构，并将其与相关生长因子的受体进行比较。我们回顾了已知的调节受体激酶活性的模式，即通过其自身磷酸化（在酪氨酸残基上）或通过其他激酶对其磷酸化（在丝氨酸和苏氨酸残基上）。鉴于有结果表明在胰岛素抵抗状态下激酶活性降低，我们讨论受体激酶活性在激素信号转导中的作用。最后，介绍了鉴定胰岛素受体激酶天然底物的研究。评估了这些磷酸化底物在介导胰岛素作用中可能的生理作用。
