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Blood, Vol. 93 No. 8 (April 15), 1999:
pp. 2578-2585
Erythropoietin Induces the Tyrosine Phosphorylation of GAB1 and Its
Association With SHC, SHP2, SHIP, and Phosphatidylinositol 3-Kinase
Carinne Lecoq-Lafon,
Frédérique Verdier,
Serge Fichelson,
Stany Chrétien,
Sylvie Gisselbrecht,
Catherine Lacombe, and
Patrick Mayeux
From the Institut Cochin de Génétique Moléculaire
(ICGM), Institut National de la Santé et de la Recherche
Médicale (INSERM U363), the Service d'Hématologie, the
Laboratoire d'Hématopoïèse, Site Transfusionnel,
Hôpital Cochin, Université René
Descartes, Paris, France; and the Institut National de la Transfusion
Sanguine (INTS), Paris, France.
Five tyrosine-phosphorylated proteins with molecular masses of 180, 145, 116, 100, and 70 kD are associated with phosphatidylinositol 3-kinase (PI 3-kinase) in erythropoietin (Epo)-stimulated UT-7 cells.
The 180- and 70-kD proteins have been previously shown to be IRS2 and
the Epo receptor. In this report, we show that the 116-kD protein is
the IRS2-related molecular adapter, GAB1. Indeed, Epo induced the
transient tyrosine phosphorylation of GAB1 in UT-7 cells. Both kinetics
and Epo dose-response experiments showed that GAB1 tyrosine
phosphorylation was a direct consequence of Epo receptor activation.
After tyrosine phosphorylation, GAB1 associated with the PI 3-kinase,
the phosphotyrosine phosphatase SHP2, the phosphatidylinositol 3,4,5 trisphosphate 5-phosphatase SHIP, and the molecular adapter SHC. GAB1
was also associated with the molecular adapter GRB2 in unstimulated
cells, and this association dramatically increased after Epo
stimulation. Thus, GAB1 could be a scaffold protein able to couple the
Epo receptor activation with the stimulation of several intracellular
signaling pathways. Epo-induced tyrosine phosphorylation of GAB1 was
also observed in normal human erythroid progenitors isolated from cord blood. Granulocyte-macrophage colony-stimulating factor (GM-CSF) and
thrombopoietin (TPO) also induced the tyrosine phosphorylation of GAB1
in UT-7 cells, indicating that this molecule participates in the signal
transduction of several cytokine receptors.
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