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Erythropoietin stimulates the tyrosine phosphorylation of Shc and its
association with Grb2 and a 145-Kd tyrosine phosphorylated protein
JE Damen, L Liu, RL Cutler and G Krystal
Terry Fox Laboratory, B.C. Cancer Agency, Vancouver, Canada.
Although the erythropoietin receptor (EpR) lacks a tyrosine kinase
consensus sequence within its proline-rich intracellular domain, addition
of its ligand to Ep-responsive cells stimulates the rapid and transient
tyrosine phosphorylation of a number of cellular proteins. The
characterization of these phosphorylatable substrates, which include 5
major phosphoproteins with molecular masses of approximately 145, 130, 97,
72, and 56 Kd is an essential step in understanding the signal transduction
pathways used by Ep. Recently, we and others have shown that the major
72-Kd tyrosine phosphorylated protein is the EpR itself. We now report,
using both murine DA-3 and human MO7E cell lines engineered to express high
levels of biologically responsive EpRs (and designated DA-ER and MO7-ER,
respectively), that the major 56-Kd tyrosine phosphorylated protein is the
recently identified SH2- containing protein, p52shc. Interestingly, in
Ep-stimulated cells, anti- Shc antibodies coprecipitate the major 145-Kd
tyrosine phosphorylated protein in both DA-ER and MO7-ER cells. Tyrosine
phosphorylation of both proteins is detectable within 30 seconds of
incubation with Ep at 37 degrees C, reaches a maximum between 2 and 5
minutes, and declines by 30 minutes. In addition, tyrosine phosphorylated
Shc appears capable of associating with the activated EpR, but this could
only be shown in MO7-ER cells. Lastly, as has been shown previously with
the tyrosine kinase containing receptors for epidermal growth factor,
platelet derived growth factor, and insulin, activation of the EpR leads to
the association of p52shc with the 25-Kd polypeptide, Grb2. Taken together,
our data suggest that the previously reported increases in rasGTP observed
with Ep result, in part, from the tyrosine phosphorylation of Shc and its
association with Grb2 and/or a tyrosine phosphorylated 145- Kd protein.
Volume 82,
Issue 8,
pp. 2296-2303,
10/15/1993
Copyright © 1993 by The American Society of Hematology
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