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(Received for publication, June 10, 1997, and in revised form, August 27, 1997)
From the Friedrich Miescher Institute, CH-4002 Basel,
Switzerland
We investigated the activation of the Ras/ERK
signaling pathway by 12-O-tetradecanoylphorbol-13-acetate
(TPA) in NIH3T3 fibroblasts. Interestingly, the activation was
suppressed not only by dominant negative Raf-1 but also by dominant
negative Ras and SOS. Further analysis revealed that TPA treatment
induced, dependently on protein kinase C, the mobility shift of
p66shc in SDS-polyacrylamide gel electrophoresis, which could
be prevented by treatment of the Shc immunoprecipitate with
serine/threonine-specific protein phosphatase 1 (PP1) or 2A (PP2A).
Phosphoamino acid analysis of Shc showed that unlike growth
factor-induced Shc phosphorylation, where Shc is mainly phosphorylated
at tyrosine residues, TPA-induced phosphorylation was only at serine
residues. Like growth factor-induced Shc phosphorylation, which leads
to the association of Shc with Grb2, TPA also induced this association,
but, correspondingly to the above results, the TPA-induced association
was disrupted by in vitro treatment of the Shc
immunoprecipitate with PP1. Taken together, these results suggest that
the TPA signal was fed at or upstream of Shc to activate the Ras/ERK
signaling pathway involving serine phosphorylation of Shc.
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