The PI3K-PDK1 connection: more than just a road to PKB

被引：1359

作者：

Vanhaesebroeck, B

Alessi, DR

机构：

[1] Ludwig Inst Canc Res, Cell Signalling Grp, London W1P 8BT, England

[2] Univ Dundee, Dept Biochem, MRC, Prot Phosphorylat Unit, Dundee DD1 5EH, Scotland

来源：

BIOCHEMICAL JOURNAL | 2000年 / 346卷 / pt 3期

关键词：

AGC kinase; Akt; apoptosis; lipid; phosphorylation;

D O I：

10.1042/0264-6021:3460561

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphoinositide 3-kinases (PI3Ks) generate specific inositol lipids that have been implicated in the regulation of cell growth, proliferation, survival, differentiation and cytoskeletal changes. One of the best characterized targets of PI3K lipid products is the protein kinase Akt or protein kinase B (PKB). In quiescent cells, PKB resides in the cytosol in a low-activity conformation. Upon cellular stimulation, PKB is activated through recruitment to cellular membranes by PI3K lipid products and phosphorylation by 3'-phosphoinositide-dependent kinase-1 (PDK1). Here we review the mechanism by which PKB is activated and the downstream actions of this multifunctional kinase. We also discuss the evidence that PDK1 may be involved in the activation of protein kinases other than PKB, the mechanisms by which this activity of PDK1 could be regulated and the possibility that some of the currently postulated PKB substrates targets might in fact be phosphorylated by PDK1-regulated kinases other than PKB.

引用

收藏

页码：561 / 576

页数：16

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