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Erythropoietin activates Raf1 by an Shc-independent pathway in CTLL-EPO- R
cells
DL Barber, CN Corless, K Xia, TM Roberts and AD D'Andrea
Division of Pediatric Oncology, Dana-Farber Cancer Institute, Harvard
Medical School, Boston, MA, USA.
Stimulation of the erythropoietin receptor (EPO-R) or the interleukin-2
receptor (IL-2-R) by their respective ligands has been reported to activate
tyrosine phosphorylation of the cytoplasmic protein, Shc. We have recently
characterized a cell line, CTLL-EPO-R, that contains functional
cell-surface receptors for both EPO and IL-2. Although stimulation with
IL-2 or IL-15 resulted in the rapid, dose-dependent tyrosine
phosphorylation of Shc, stimulation with EPO failed to activate Shc. EPO,
IL-2, and IL-15 activated the tyrosine phosphorylation of the adaptor
protein, Shp2, and the association of Shp2/Grb2/cytokine receptor
complexes. In addition, EPO, IL-2, and IL- 15 activated Raf1 and ERK2,
demonstrating that the Raf1/MEK/MAP kinase pathway was activated. These
results indicate that multiple biochemical pathways are capable of
conferring a mitogenic signal in CTLL-EPO-R. EPO can activate the
Raf1/MEK/MAP kinase pathway via Shc-dependent or Shc-independent pathways,
and Shc activation is not required for EPO- dependent cell growth in
CTLL-EPO-R.
Volume 89,
Issue 1,
pp. 55-64,
01/01/1997
Copyright © 1997 by The American Society of Hematology
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