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- W2907046134 abstract "This chapter focuses on research aimed at understanding the mechanism by which PtdIns(3,4,5)P 3 regulates one branch of its downstream signaling pathways, namely enabling PDK1 to phosphorylate and activate a group of serine/threonine protein kinases that belong to the AGC subfamily of protein kinases. These include isoforms of PKB, p70 ribosomal S6 kinase (S6K), serum- and glucocorticoid-induced protein kinase (SGK), p90 ribosomal S6 kinase (RSK), and protein kinase C (PKC) isoforms. Once these diverse AGC kinase members are activated, they phosphorylate and change the activity and function of key regulatory proteins that control processes such as cell proliferation and survival as well as cellular responses to insulin. The results discussed in this chapter also provide a framework within which drugs could be developed to inhibit the PDK1/AGC kinase pathway to treat forms of cancers in which this pathway may be constitutively activated. Indeed, it is now estimated that PTEN is mutated in up to 30% of all human tumors, resulting in elevated PtdIns(3,4,5)P 3 levels and hence PKB and S6K activity which are likely to contribute to the proliferation and survival of these tumors. It could be envisaged that a PDK1 inhibitor would be effective at reducing the PKB and S6K activities that contribute to growth and survival of these tumors." @default.
- W2907046134 created "2019-01-11" @default.
- W2907046134 creator A5054181982 @default.
- W2907046134 date "2003-01-01" @default.
- W2907046134 modified "2023-09-24" @default.
- W2907046134 title "Role of PDK1 in Activating AGC Protein Kinase" @default.
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