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J Biol Chem, Vol. 274, Issue 35, 24469-24474, August 27, 1999
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From the Several signaling cascades are activated during
engagement of the erythropoietin receptor to mediate the biological
effects of erythropoietin. The members of the insulin receptor
substrate (IRS) family of proteins play a central role in signaling for various growth factor receptors and cytokines by acting as docking proteins for the SH2 domains of signaling elements, linking cytokine receptors to diverse downstream pathways. In the present study we
provide evidence that the recently cloned IRS-related proteins, Gab1
and Gab2, of the Gab family of proteins, are rapidly phosphorylated on
tyrosine during erythropoietin treatment of erythropoietin-responsive cells and provide docking sites for the engagement of the SHP2 phosphatase and the p85 subunit of the phosphatidylinositol 3'-kinase. Furthermore, our data show that Gab1 is the primary IRS-related protein
activated by erythropoietin in primary erythroid progenitor cells. In
studies to identify the erythropoietin receptor domains required for
activation of Gab proteins, we found that tyrosines 425 and 367 in the
cytoplasmic domain of the erythropoietin receptor are required for the
phosphorylation of Gab2. Taken together, our data demonstrate that Gab
proteins are engaged in erythropoietin signaling to mediate downstream
activation of the SHP2 and phosphatidylinositol 3'-kinase pathways and
possibly participate in the generation of the erythropoietin-induced
mitogenic responses.
Section of Hematology-Oncology, University
of Illinois at Chicago and West Side Veterans Affairs Medical Center,
Chicago, Illinois 60607, the ¶ Department of Pharmacology, Medical
College of Virginia, Richmond, Virginia 23298, the Terry Fox
Laboratory, British Columbia Cancer Research Centre, Vancouver, British
Columbia V5Z 1L3, Canada, the ** Lerner Research Institute, Cleveland
Clinic Foundation, Cleveland, Ohio 44195, and the
Division of Molecular Oncology, Biomedical
Research Center, Osaka University Graduate School of Medicine,
Osaka 565-0871, Japan
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