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    Biochem Biophys Res Commun. 2000 Oct 14;277(1):195-9.

    Flt3 ligand induces tyrosine phosphorylation of gab1 and gab2 and their association with shp-2, grb2, and PI3 kinase.

    Zhang S, Broxmeyer HE.

    Source

    Department of Microbiology/Immunology, Indiana University School of Medicine, Indianapolis, Indiana 46202, USA.

    Abstract

    The receptor tyrosine kinase Flt3 has been shown to play an important role in proliferation, differentiation, and survival of hematopoietic stem and progenitor cells. Although some postreceptor signaling events of Flt3 have been characterized, the involvement of Gab family proteins in Flt3 signaling is not known. In this study, we show that both Gab1 and Gab2 are rapidly tyrosine phosphorylated after Flt3 ligand stimulation of Flt3 ligand-responsive cells. They interact with tyrosine-phosphorylated Shp-2, p85, Grb2, and Shc. The results suggest that Gab proteins are engaged in Flt3 signaling to mediate downstream activation of Shp-2 and PI3 kinase pathways and possibly the Ras/Raf/MAPK pathway.

    Copyright 2000 Academic Press.

    PMID:
    11027663
    [PubMed - indexed for MEDLINE]

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