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Specific involvement of tyrosine 764 of human granulocyte colony-
stimulating factor receptor in signal transduction mediated by
p145/Shc/GRB2 or p90/GRB2 complexes
JP de Koning, AM Schelen, F Dong, C van Buitenen, BM Burgering, JL Bos, B Lowenberg and IP Touw
Institute of Hematology, Erasmus University, Rotterdam, The Netherlands.
Signal transduction from the granulocyte colony-stimulating factor receptor
(G-CSF-R) occurs via multiple pathways, one of which involves activation of
p21Ras and mitogen-activated protein kinase. The SH2 domain-containing
proteins Shc and GRB2 have been implicated in this latter signaling route.
We studied the role of these proteins in signal transduction from wild type
(WT) G-CSF-R, C-terminal deletion mutants, and tyrosine-to-phenylalanine
substitution mutants in transfectants of the mouse pro-B cell line, BAF3.
G-CSF stimulation of BAF3 cells expressing WT G-CSF-R induced tyrosine
phosphorylation of Shc. Anti-Shc antibodies co-immunoprecipitated
tyrosine-phosphorylated 145-kD proteins (p145), whereas GRB2
immunoprecipitates contained phosphorylated Shc, Syp, and proteins of 145
and 90 kD (p90). Neither of these complexes were detected after activation
of a C-terminal deletion mutant of G-CSF-R that lacked all four conserved
cytoplasmic tyrosine residues. G-CSF induced formation of Syp/GRB2
complexes in all the tyrosine-substitution mutants, suggesting that this
association did not depend on the presence of single specific tyrosine
residues in G- CSF-R. In contrast, tyrosine 764 of G-CSF-R appeared to be
exclusively required for tyrosine phosphorylation of Shc and its
association with p145 and GRB2. In addition, tyrosine 764 also specifically
mediated binding of GRB2 to p90 without the involvement of Shc. These
findings indicate that tyrosine 764 of G-CSF-R has a prominent role in
G-CSF signal transduction.
Volume 87,
Issue 1,
pp. 132-140,
01/01/1996
Copyright © 1996 by The American Society of Hematology
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