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A tyrosine-phosphorylated protein of 140 kD is constitutively associated
with the phosphotyrosine binding domain of Shc and the SH3 domains of Grb2
in acute myeloid leukemia cells
M Jucker, CA Schiffer and RA Feldman
Department of Microbiology and Immunology, University of Maryland School of
Medicine, Baltimore 21201, USA.
The Shc gene encodes three proteins that have been implicated as mediators
of signal transduction from growth factor receptors and nonreceptor
tyrosine kinases to Ras. Overexpression of Shc in established murine
fibroblasts results in oncogenic transformation, indicating that Shc has
oncogenic potential. Shc proteins contain a carboxy terminal SH2 domain and
a novel non-SH2 phosphotyrosine-binding (PTB) domain that specifically
recognizes a phosphorylated NPXpY motif in target proteins such as the
epidermal growth factor receptor. We show here that Shc is constitutively
tyrosine-phosphorylated in all primary acute myeloid leukemias analyzed and
that, in some of these leukemias, Shc is associated through its PTB domain
with a tyrosine- phosphorylated protein of 140 kD (p140) in vivo. In
factor-dependent cells, this 140-kD protein can be tyrosine-phosphorylated
in vitro in response to cytokines involved in myeloid proliferation and
differentiation, ie, granulocyte-macrophage colony-stimulating factor and
colony-stimulating factor-1. A similar or identical protein of 140 kD is
constitutively bound to the C-terminal SH3 domain of Grb2 in the same acute
myeloid leukemias. In addition to p140, other tyrosine- phosphorylated
proteins of 61 and 200 kD are constitutively associated with Shc in some of
the leukemias analyzed. Our results implicate Shc, Grb2, p140, and
additional tyrosine-phosphorylated proteins of 61 and 200 kD in signalling
of acute myeloid leukemia cells.
Volume 89,
Issue 6,
pp. 2024-2035,
03/15/1997
Copyright © 1997 by The American Society of Hematology
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