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Cited by 1,644

The DOI matches its OpenAlex record; 179 of the 179 references it cites were found in a registry or an index.

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

Open access
Bart Vanhaesebroeck, Dario R. Alessi·2000·Biochemical Journal

Abstract

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.

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OpenAlex · 10.1042/0264-6021:3460561

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Metadata

Authors
Vanhaesebroeck, B., & Alessi, D. R.
Venue
Biochemical Journal
Publisher
Portland Press
Published
2000-03-07
Volume
346
Issue
3
Pages
561-561
ISSN
0264-6021 (ISSN-L)
OpenAlex
W2039193709
Cited by
1,644
References
179
FWCI
50.13
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The PI3K‒PDK1 connection: more than just a road to PKB. https://app.cochat.ai/papers/10.1042/0264-6021:3460561
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Vanhaesebroeck, B., & Alessi, D. R. (2000). The PI3K‒PDK1 connection: more than just a road to PKB. Biochemical Journal. https://doi.org/10.1042/0264-6021%3A3460561

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.