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Steel factor induces serine phosphorylation of Stat3 in human growth
factor-dependent myeloid cell lines
A Gotoh, H Takahira, C Mantel, S Litz-Jackson, HS Boswell and HE Broxmeyer
Department of Medicine and Microbiology/Immunology Indiana University
School of Medicine, Indianapolis, 46202-5121, USA.
Steel factor (SLF) acts synergistically with various hematopoietic growth
factors that use the Jak-Stat pathways in vivo and in vitro, although the
contribution by SLF to this pathway is unknown. We show here that SLF
induces time- and dose-dependent phosphorylation of Stat3 in the human
growth factor-dependent cell lines MO7e and TF-1. This phosphorylation
occurs exclusively on serine residues. Simultaneous stimulation with SLF
plus other cytokines that induce tyrosine phosphorylation of Stat3, such as
interleukin-9 (IL-9) in MO7e cells or IL-6 in TF-1 cells, resulted in
tyrosine phosphorylation and enhanced serine phosphorylation of Stat3.
Serine phosphorylation alone did not promote nuclear translocation or DNA
binding activity to the sis- inducible element of Stat3. However,
costimulation with SLF plus IL-9 in MO7e cells resulted in the nuclear
translocation of serine- hyperphosphorylated Stat3. Serine phosphorylation
of Stat3 was also observed by the stimulation of cells with
granulocyte-macrophage colony- stimulating factor and IL-3, which do not
induce tyrosine phosphorylation of Stat3. These results suggest that SLF
might modulate the Jak-Stat3 pathway by serine phosphorylation and that the
Jak-Stat pathway may be differentially regulated by the combinational
stimulation of two or more cytokines.
Volume 88,
Issue 1,
pp. 138-145,
07/01/1996
Copyright © 1996 by The American Society of Hematology
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