Regulation of the p70 S6 kinase by phosphorylation in vivo. Analysis using site-specific anti-phosphopeptide antibodies.

The Journal of Biological Chemistry
Q P WengJ Avruch

Abstract

The p70 S6 kinase is activated by diverse stimuli through a multisite phosphorylation directed at three separate domains as follows: a cluster of (Ser/Thr) Pro sites in an autoinhibitory segment in the noncatalytic carboxyl-terminal tail; Thr-252 in the activation loop of the catalytic domain; and Ser-394 and Thr-412 in a segment immediately carboxyl-terminal to the catalytic domain. Phosphorylation of Thr-252 in vitro by the enzyme phosphatidylinositol 3-phosphate-dependent kinase-1 or mutation of Thr-412 --> Glu has each been shown previously to engender some activation of the p70 S6 kinase, whereas both modifications together produce 20-30-fold more activity than either alone. We employed phospho-specific anti-peptide antibodies to examine the relative phosphorylation at several of these sites in wild type and various p70 mutants, in serum-deprived cells, and in response to activators and inhibitors of p70 S6 kinase activity. Substantial phosphorylation of p70 Thr-252 and Ser-434 was present in serum-deprived cells, whereas Thr-412 and Thr-444/Ser-447 were essentially devoid of phospho-specific immunoreactivity. Activation of p70 by insulin was accompanied by a coordinate increase in phosphorylation at all sites examined, to...Continue Reading

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Citations

Sep 27, 2002·Genesis : the Journal of Genetics and Development·Hélène Barcelo, Mary J Stewart
Dec 22, 1999·Biochemical and Biophysical Research Communications·L A BervenM F Crouch
Jun 7, 2008·European Journal of Applied Physiology·Louise DeldicqueMarc Francaux
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Aug 5, 2009·The Journal of Biological Chemistry·Antonella CaccamoSalvatore Oddo
Jul 3, 2009·The Journal of Biological Chemistry·Malik M KeshwaniThomas K Harris
Dec 7, 2010·The Journal of Biological Chemistry·Irantzu TatoJose Luis Rosa
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Nov 10, 2007·The Journal of Clinical Investigation·David M SelvaGeoffrey L Hammond

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