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        Measurement of Phosphoinositide 3-Kinase Activation by Interleukins

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        Phosphoinositide 3-kinases (PI 3-kinases) are an evolutionarily conserved family of lipid kinases that have attracted much attention over the past 10 years or so (reviewed in ref. 1 ). Three PI 3-kinase classes have been defined on the basis of primary structure, regulation, and their in vitro lipid substrate specificity. Class I PI 3-kinases interact with Ras and form heterodimeric complexes with adaptor proteins that link them to different upstream signaling events ( 1 ). They are able to convert phosphatidylinositol (PtdIns), PtdIns( 4 ) P , and PtdIns( 4 , 5 ) P 2 into PtdIns( 3 ) P , PtdIns( 3 , 4 ) P 2 , and PtdIns( 3 , 4 , 5 ) P 3 , respectively, by phosphorylating the D-3 position of the inositol head groups of phosphoinositide lipids (collectively known as D-3 phosphoinositide lipids and shown in Fig. 1 ) ( 1 , 2 ).
        Fig. 1.  ( A ) Schematic representation of the structure of D-3 phosphoinositide lipids. ( B ) Routes for synthesis of PtdIns( 3 ) P , PtdIns( 3 , 5 ) P 2 , PtdIns( 3 , 4 ) P 2 , and PtdIns( 3 , 4 , 5 ) P 3 .

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