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Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 1934-1941
Cytoplasmic Domains of the Leukemia Inhibitory Factor Receptor
Required for STAT3 Activation, Differentiation, and Growth
Arrest of Myeloid Leukemic Cells
Mikio Tomida,
Toshio Heike, and
Takashi Yokota
From the Saitama Cancer Center Research Institure, Ina, Saitama,
Japan; and the Department of Stem Cell Regulation, Institute of Medical
Science, University of Tokyo, Shirokanedai, Minato-ku, Tokyo, Japan.
Leukemia inhibitory factor (LIF) induces growth arrest and
macrophage differentiation of mouse myeloid leukemic cells through the
functional LIF receptor (LIFR), which comprises a heterodimeric complex
of the LIFR subunit and gp130. To identify the regions within the
cytoplasmic domain of LIFR that generate the signals for growth arrest,
macrophage differentiation, and STAT3 activation independently of
gp130, we constructed chimeric receptors by linking the transmembrane
and intracellular regions of mouse LIFR to the extracellular domains of
the human granulocyte macrophage colony-stimulating factor receptor
(hGM-CSFR)  and  c chains. Using the full-length cytoplasmic
domain and mutants with progressive C-terminal truncations or point
mutations, we show that the two membrane-distal tyrosines with the YXXQ
motif of LIFR are critical not only for STAT3 activation, but also for
growth arrest and differentiation of WEHI-3B D+ cells. A
truncated STAT3, which acts in a dominant negative manner was
introduced into WEHI-3B D+ cells expressing
GM-CSFR-LIFR and GM-CSFRc-LIFR. These cells were not
induced to differentiate by hGM-CSF. The results indicate that STAT3
plays essential roles in the signals for growth arrest and
differentiation mediated through LIFR.
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