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• W1569502846 abstract "Insulin increases the net uptake of glucose from the blood and conversion of glucose to glycogen and triglyceride, at the same time inhibiting their breakdown. The actions of insulin must be mediated through a mechanism that involves autophosphorylation of the receptor. The discovery of protein kinase B (PKB) and the 3-phosphorylated inositol lipids that act as signaling molecules provided the key to this mechanism. 3-phosphorylated inositol lipids are the products of the phosphoinositide 3-kinases (PI 3-kinases) that phosphorylate PI and its derivatives PI(4)P and PI(4,5)P 2 position to give PI(3)P, PI(3,4)P 2 , and PI (3,4,5)P 3 . Receptors for growth factors activate the PI 3-kinases through interaction with the SH2 domain of the p85 regulatory subunits. Protein kinase B (PKB), a cellular serine–threonine protein kinase, differs from other protein kinases because it contains a pleckstrin homology (PH) domain. PI(3,4,5)P 3 was found to be the activator of PKB, which plays two roles in mechanism of this activation: the lipid head-group binding to a PH domain in the N-terminal segment of PKB, and the other involving a soluble protein kinase, 3-phosphoinositide dependent protein kinase (PDK1). Binding of insulin to its receptor results in prolonged activation of PI 3-kinase, the activation of PI 3-kinase is mediated through its interaction with a molecule that is a substrate of the insulin receptor. Because the receptor is a dimer, the possibility exists that ligand binding induces a domain movement that brings about autophosphorylation. This is followed by phosphorylation of a number of insulin receptor substrates (IRS)." @default.
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• W1569502846 date "2002-01-01" @default.
• W1569502846 modified "2023-09-27" @default.
• W1569502846 title "Phosphoinositide 3-kinases, protein kinase B and signalling through the insulin receptor" @default.
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• W1569502846 doi "https://doi.org/10.1016/b978-012289631-6/50033-8" @default.
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