p70S6K is responsible for the phosphorylation of 40S ribosomal protein S6 and is ubiquitously expressed in human adult tissues.p70S6K is activated by serum stimulation and this activation is inhibited by wortmannin and rapamycin. p70S6k activity undergoes changes in the cell cycle and increases 20-fold in G1 cells released from G0. p70S6K activation requires sequential phosphorylations at proline-directed residues in the putative autoinhibitory pseudosubstrate domain, as well as threonine 389, a site phosphorylated by phosphoinositide-dependent kinase 1 (PDK-1).
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Critical reviews in biochemistry and molecular biology, 29(6), 385-413 (1994-01-01)
Activation of cell growth leads to the multiple phosphorylation of 40S ribosomal protein S6. The kinase responsible for controling this event is termed p70s6k/p85s6k. Both isoforms of the kinase are derived from a common gene activated by a complex set
The Journal of biological chemistry, 271(2), 963-971 (1996-01-12)
We show here using synchronized Swiss mouse 3T3 fibroblasts that p70 S6 kinase (p70S6k) and mitogen-activated protein kinases (p42mapk/p44mapk) are not only activated at the G0/G1 boundary, but also in cells progressing from M into G1. p70S6k activity increases 20-fold
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