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Tryptophan 650 of human granulocyte colony-stimulating factor (G-CSF)
receptor, implicated in the activation of JAK2, is also required for G-
CSF-mediated activation of signaling complexes of the p21ras route
RM Barge, JP de Koning, K Pouwels, F Dong, B Lowenberg and IP Touw
Institute of Hematology, Erasmus University, Rotterdam, The Netherlands.
Granulocyte colony-stimulating factor (G-CSF) induces rapid phosphorylation
of JAK kinases as well as activation of the p21ras route through
interaction with its specific receptor (G-CSF-R). The cytoplasmic
membrane-proximal region of G-CSF-R (amino acids 631 to 684) is necessary
for proliferation induction and activation of JAK2. In contrast, activation
of Shc and Syp, signaling molecules implicated in the p21ras signaling
route, depends on the phosphorylation of tyrosine residues located in the
membrane-distal region (amino acids 685 to 813) of G-CSF-R. We investigated
whether G-CSF-induced activation of signaling complexes of the p21ras route
depends on the function of the membrane-proximal cytoplasmic region of
G-CSF-R. A G- CSF-R mutant was constructed in which tryptophan 650 was
replaced by arginine and expressed in BAF3 cells (BAF/W650R). In contrast
to BAF3 cell transfectants expressing wild-type G-CSF-R, BAF/W650-R cells
did not proliferate and did not show activation of JAK2, STAT1, or STAT3 in
response to G-CSF. Immunoprecipitations with anti-Shc and anti-Grb2
antisera showed that mutant W650R also failed to activate Syp and Shc.
These data indicate that the membrane-proximal cytoplasmic domain of G-
CSF-R is not only crucial for proliferative signaling and activation of
JAK2 and STATs, but is also required for activation of the p21ras route,
which occurs via the membrane-distal region of G-CSF-R.
Volume 87,
Issue 6,
pp. 2148-2153,
03/15/1996
Copyright © 1996 by The American Society of Hematology
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