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Activation of the erythropoietin receptor by the Friend spleen focus-
forming virus gp55 glycoprotein induces constitutive protein tyrosine
phosphorylation
MO Showers, JF Moreau, D Linnekin, B Druker and AD D'Andrea
Division of Hematology-Oncology, Dana-Farber Cancer Institute, Harvard
Medical School, Boston, MA 02115.
The erythropoietin receptor (EPO-R) can be activated to signal cell growth
by binding either EPO or gp55, the Friend spleen focus-forming virus (SFFV)
glycoprotein. EPO binding induces tyrosine kinase activity and rapid
tyrosine phosphorylation of several cellular substrates. To test for
gp55-induced tyrosine kinase activity, we performed immunoblots on two
murine cell lines that stably express EPO-R and gp55. Stimulation of the
parental cell line, Ba/F3, with murine interleukin-3 (IL-3) resulted in
rapid, dose-dependent tyrosine phosphorylation of a 97-Kd substrate.
Stimulation with IL-3 or EPO of the Ba/F3 cells expressing the recombinant
EPO-R (Ba/F3-EPO-R) resulted in tyrosine phosphorylation of the same p97
substrate. These latter cells, when transformed to growth
factor-independence by the Friend gp55 glycoprotein, exhibited constitutive
tyrosine phosphorylation of the 97-Kd substrate. Other growth
factor-independent Ba/F3 subclones, transformed with either the
oncoprotein, v-abl, or with a constitutively activated EPO-R, also had
constitutive phosphorylation of a 97-Kd substrate. In CTLL-2-EPO-R cells, a
T-lymphocyte line stably transfected with the EPO-R, the 97-Kd substrate
was tyrosine- phosphorylated in response to IL-2 or EPO. The 97-Kd protein
was constitutively phosphorylated in CTLL-2-EPO-R-gp55 cells. In
conclusion, a 97-Kd protein found in two murine cell lines is tyrosine-
phosphorylated in response to multiple growth factors and viral
oncoproteins, and appears to be a central phosphoprotein in signal
transduction.
Volume 80,
Issue 12,
pp. 3070-3078,
12/15/1992
Copyright © 1992 by The American Society of Hematology
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