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J. Biol. Chem., Vol. 268, Issue 29, 21463-21465, 10, 1993
RL Cutler, L Liu, JE Damen and G Krystal
The identification and characterization of proteins that become
tyrosine-phosphorylated in response to growth factor stimulation is
critical to furthering our understanding of the signal transduction
pathways involved in regulating cell proliferation and differentiation. In
this report we demonstrate that interleukin-3, erythropoietin, and steel
factor all induce the tyrosine phosphorylation of the SH2 containing
protein, p52shc. These studies were carried out with various human and
murine cell lines to document that this is a common event in hemopoietic
cells. We also show that upon tyrosine phosphorylation, p52shc becomes
associated with the adaptor protein, Grb2. The formation of this complex
may directly link tyrosine phosphorylation events to Ras activation in
hemopoietic progenitors and may be a critical step in stimulating these
cells to transit through G1 into S phase.
Multiple cytokines induce the tyrosine phosphorylation of Shc and its association with Grb2 in hemopoietic cells
Terry Fox Laboratory, British Columbia Cancer Research Centre, Vancouver, Canada.
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