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Erythropoietin and interleukin-3 activate tyrosine phosphorylation of CBL
and association with CRK adaptor proteins
DL Barber, JM Mason, T Fukazawa, KA Reedquist, BJ Druker, H Band and AD D'Andrea
Ontario Cancer Institute, Division of Cellular and Molecular Biology,
Toronto, Canada.
Transformation of hematopoietic cells by the Bcr-abl oncoprotein leads to
constitutive tyrosine phosphorylation of a number of cellular polypeptides
that function in normal growth factor-dependent cell proliferation. Recent
studies have shown that the CrkL adaptor protein and the Cbl
protooncoprotein are constitutively tyrosine phosphorylated and form a
preformed complex in cells expressing Bcr-abl. In the current study, we
have examined cytokine-dependent tyrosine phosphorylation of Cbl and its
association with Crk proteins. Erythropoietin (EPO) and interleukin-3
induced a dose and time- dependent tyrosine phosphorylation of Cbl in both
EPO-dependent Ba/F3 and DA-3 transfectants, and the erythroid cell line
HCD-57. Furthermore, once phosphorylated, Cbl associated with Crk adaptor
proteins. Of the three Crk isoforms expressed in hematopoietic cells (CrkL,
CrkII, and CrkI), tyrosine phosphorylated Cbl binds preferentially to CrkL
and CrkII. The amount of Cbl associated with CrkL and CrkII exceeded the
fraction of Cbl associated with Grb2 indicating that unlike other receptor
systems, the Cbl-Crk association represents the dominant complex of Cbl in
growth factor-stimulated hematopoietic cells. In factor-dependent
hematopoietic cell lines, CrkL constitutively associated with the guanine
nucleotide release factor, C3G, which is known to interact via Crk
src-homology 3 (SH3) domains. Our data suggest that the inducible Cbl-Crk
association is a proximal component of a signaling pathway downstream of
multiple cytokine receptors.
Volume 89,
Issue 9,
pp. 3166-3174,
05/01/1997
Copyright © 1997 by The American Society of Hematology
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