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(Received for publication, April 1, 1996, and in revised form, July 19, 1996)
From the § Melbourne Tumour Biology Branch, The cytoplasmic tyrosine residues of many growth
factor receptors have been shown to be important for receptor signal
transduction via the recruitment of proteins containing
phosphotyrosine-binding domains. This study demonstrates the importance
of specific tyrosine residues in the granulocyte colony-stimulating
factor (G-CSF) receptor cytoplasmic domain in G-CSF-induced macrophage
cell differentiation. Site-directed mutagenesis was used to generate a
series of G-CSF receptor (G-CSF-R) mutants in which the tyrosine
residues were replaced with phenylalanine either singly or in
combination. The mouse myeloid leukemic cell line (M1) transfected with
G-CSF-R cDNA can be induced to differentiate into macrophages in
response to G-CSF. The effect of the tyrosine mutations on this
differentiation response was assessed by examining cell morphology and
differentiation in soft agar colony assays. Although three of the four
cytoplasmic tyrosine residues appeared to contribute to the
differentiation response, mutation of a single residue
(Tyr744) significantly reduced the ability of the M1 cells
to differentiate. The STAT family of signaling molecules (Stat1, Stat3,
and Stat5) were activated by G-CSF in M1 cells expressing those G-CSF-R
tyrosine mutants unable to mediate G-CSF-induced differentiation.
Furthermore, activation of STAT proteins was shown to occur in the
absence of all four cytoplasmic tyrosine residues, suggesting an
alternative mechanism for STAT activation other than direct interaction
with receptor phosphotyrosines.
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26947-26953
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Department of Medicine,
University of Melbourne, Victoria 3050, Australia
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