Abstract
Interleukin-2 induces a serine-phosphorylated phosphatidylinositol 3 kinase activity in the mouse T cell line TS1 alpha beta. Moreover, protein kinase C (PKC) zeta directly or indirectly associates with the phosphatidylinositol 3 kinase and the association appears to be necessary for the serine-phosphorylated phosphatidylinositol 3 kinase activity, since release of zeta PKC by competition of binding with peptides spanning the p110 sequence from amino acids 907 to 925 abolishes the serine-phosphorylated phosphatidylinositol 3 kinase activity. This kinase activity is also blocked when zeta PKC expression is inhibited by antisense oligonucleotide. Inhibition of phosphatidylinositol 3 kinase activity by wortmannin does not abolish zeta PKC association.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Cell Line
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Enzyme Activation / drug effects
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Humans
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Interleukin-2 / pharmacology*
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Mice
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Molecular Sequence Data
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Phosphatidylinositol 3-Kinases
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Phosphoserine / immunology
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Phosphotransferases (Alcohol Group Acceptor) / drug effects*
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Phosphotransferases (Alcohol Group Acceptor) / immunology
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Phosphotransferases (Alcohol Group Acceptor) / metabolism*
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Protein Binding
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Protein Kinase C / drug effects*
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Protein Kinase C / metabolism*
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Protein Serine-Threonine Kinases / drug effects
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T-Lymphocytes / enzymology
Substances
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Interleukin-2
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Phosphoserine
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Phosphotransferases (Alcohol Group Acceptor)
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Protein Serine-Threonine Kinases
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protein kinase C zeta
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Protein Kinase C