Insulin Receptor Kinase and Insulin Action
Insulin has been shown to elicit its numerous biological effects by interacting with a specific cell-surface receptor. The insulin receptor structure has been elucidated through a variety of techniques (Van Obberghen 1984), and more recently, the amino acid sequence of the human insulin receptor precursor has been unravelled by recombinant DNA technology (Ullrich et al. 1985; Ebina et al. 1985). Despite this progress the molecular mechanism of insulin action is still not entirely comprehended regarding the events following receptor binding and leading to the ultimate cellular responses. However, over the years considerable evidence has been gathered indicating that reversible phosphorylation contributes to the mechanism of insulin action (Denton 1986). Further, a promising discovery was made by the demonstration that the insulin receptor is an insulin-sensitive protein kinase (Kasuga et al. 1982a, b, c; Van Obberghen and Kowalski 1982; Petruzzelli et al. 1982). This observation is of particular interest for our understanding of insulin- regulated processes, since it is now recognized that phosphorylation-dephospho- rylation of proteins is a mechanism whereby many cellular functions are regulated by hormones and neurotransmitters. Furthermore, protein kinases are also constituents of receptors for several growth factors, implying that receptor kinase activity may represent a general mechanism in transmembrane signalling of hormones and growth factors.
KeywordsTyrosine Vanadate Serine Trypsin Thymidine
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