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J Biol Chem, Vol. 273, Issue 24, 14962-14967, June 12, 1998
From the Laboratory of Molecular Oncology, INSERM U119,
13009 Marseille, France
The FLT3 receptor tyrosine kinase and its ligand,
FL, play an important role in early hematopoietic development. We have
found that CBLB, a recently characterized molecule closely related to the CBL protooncogene product, is phosphorylated on tyrosine(s) following FL treatment of JEA2 human pro-B cells and THP1 monocytic cells. Treatment of JEA2 cells with interleukin (IL)-7 induces CBLB
phosphorylation as well. FL and IL-7, respectively, induce and increase
association of tyrosine-phosphorylated SHC and the p85 subunit of
phosphatidylinositol 3'-kinase with CBLB. In these cells, CBLB
constitutively binds the GRB2 adaptor predominantly through its
N-terminal SH3 domain, to form a complex that is distinct from the
GRB2·CBL and GRB2·SOS1 complexes. Together with the fact that CBLB
is consistently found in blast cells from acute leukemias and in
peripheral blood mononuclear cells, this suggests that CBLB has a role
in tyrosine kinase-regulated signaling pathways in many hematolymphoid
cells.
The CBL-related Protein CBLB Participates in FLT3 and
Interleukin-7 Receptor Signal Transduction in Pro-B Cells
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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