PMID: 9445476Feb 21, 1998Paper

Phosphorylation and activation of p70s6k by PDK1

Science
N PullenG Thomas

Abstract

Activation of the protein p70s6k by mitogens leads to increased translation of a family of messenger RNAs that encode essential components of the protein synthetic apparatus. Activation of the kinase requires hierarchical phosphorylation at multiple sites, culminating in the phosphorylation of the threonine in position 229 (Thr229), in the catalytic domain. The homologous site in protein kinase B (PKB), Thr308, has been shown to be phosphorylated by the phosphoinositide-dependent protein kinase PDK1. A regulatory link between p70s6k and PKB was demonstrated, as PDK1 was found to selectively phosphorylate p70s6k at Thr229. More importantly, PDK1 activated p70s6k in vitro and in vivo, whereas the catalytically inactive PDK1 blocked insulin-induced activation of p70s6k.

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Citations

Jan 10, 2002·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Sara C Kozma, George Thomas
Apr 19, 2011·Targeted Oncology·Kevin R KellyJennifer S Carew
Mar 17, 2004·Biochimica Et Biophysica Acta·Masahito HanadaBrian A Hemmings
Aug 10, 2005·The International Journal of Biochemistry & Cell Biology·David J Glass
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Apr 21, 1999·Current Opinion in Cell Biology·S J LeeversM D Waterfield
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Aug 18, 2000·Immunology and Cell Biology·L A Berven, M F Crouch

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