Affiliation:
1. Friedrich Miescher Institute, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.
Abstract
Activation of the protein p70
s6k
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 (Thr
229
), in the catalytic domain. The homologous site in protein kinase B (PKB), Thr
308
, has been shown to be phosphorylated by the phosphoinositide-dependent protein kinase PDK1. A regulatory link between p70
s6k
and PKB was demonstrated, as PDK1 was found to selectively phosphorylate p70
s6k
at Thr
229
. More importantly, PDK1 activated p70
s6k
in vitro and in vivo, whereas the catalytically inactive PDK1 blocked insulin-induced activation of p70
s6k
.
Publisher
American Association for the Advancement of Science (AAAS)
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