The α-isoform of class II phosphoinositide 3-kinase is more effectively activated by insulin receptors than IGF receptors, and activation requires receptor NPEY motifs |
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Authors: | B Urs R A Brown S ORahilly P R Shepherd K Siddle |
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Institution: | University of Cambridge, Department of Clinical Biochemistry, Addenbrooke's Hospital, Cambridge, UK. |
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Abstract: | Little is known about the physiological role and mechanism of activation of class II phosphoinositide 3-kinases (PI3Ks), although it has been shown that the PI3K-C2alpha isoform is activated by insulin. Using chimaeric receptor constructs which can be activated independently of endogenous receptors in transfected cells, we found that PI3K-C2alpha activity was stimulated to a greater extent by insulin receptors than IGF receptors in 3T3-L1 adipocytes. Activation of PI3K-C2alpha required an intact NPEY motif in the receptor juxtamembrane domain. We conclude that PI3K-C2alpha is a candidate for participation in insulin-specific intracellular signalling. |
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Keywords: | Insulin Insulin-like growth factor Receptor Phosphoinositide 3-kinase C2α 3T3-L1 adipocyte |
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