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Rapid activation of the STAT3 transcription factor by granulocyte
colony-stimulating factor
SS Tian, P Lamb, HM Seidel, RB Stein and J Rosen
Ligand Pharmaceuticals, San Diego, CA 92121.
Granulocyte colony-stimulating factor (G-CSF) is a glycoprotein that
stimulates proliferation and differentiation of progenitor cells of
neutrophils by signaling through its receptor (G-CSFR). Although the G-
CSFR belongs to the cytokine receptor superfamily, which lacks an
intracellular kinase domain, G-CSF-induced tyrosine phosphorylation of
cellular proteins is critical for its biologic activities. We report here
that JAK1 and JAK2 tyrosine kinases are tyrosine phosphorylated in response
to G-CSF induction. We also demonstrate that the DNA-binding protein STAT3
(also called the acute-phase response factor [APRF], activated by
interleukin-6) is an early target of G-CSF-induced tyrosine
phosphorylation. G-CSF induces two DNA-binding complexes; the major complex
contains tyrosine phosphorylated STAT3 protein and the minor complex
appears to be a heterodimer of the STAT1 (previously p91, a component of
DNA-binding complexes activated by interferons) and STAT3 proteins.
Antiphosphotyrosine antibody interferes with the DNA binding activity of
activated STAT3, indicating that tyrosine phosphorylation of STAT3 is
important for the DNA binding activity. These results identify a signal
transduction pathway activated in response to G-CSF and provide a mechanism
for the rapid modulation of gene expression by G-CSF.
Volume 84,
Issue 6,
pp. 1760-1764,
09/15/1994
Copyright © 1994 by The American Society of Hematology
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