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Departments of
*
Molecular and Developmental Biology and
Clinical Oncology, Institute of Medical Science, University of Tokyo; and
Core Research for Engineering, Science, and Technology, Japan Science and Technology Corporation, Tokyo, Japan
Receptors for GM-CSF, IL-3, and IL-5 are composed of two subunits:
, which is specific for each cytokine, and ßc, which is shared by
all. Although the role of ßc in signal transduction has been
extensively studied, the role of the subunit has remained to be
clarified. To analyze the role of the human (h) GM-CSF receptor
subunit, we constructed a chimeric receptor subunit composed of
extracellular and transmembrane regions of fused with the
cytoplasmic region of ßc, designated /ß. In BA/F3 cells,
chimeric receptor composed of /ß,ß can transduce signals for
mitogen-activated protein kinase cascade activation and proliferation
in response to hGM-CSF. Although phosphorylation of Jak1 but not of
Jak2 occurred with stimulation of hGM-CSF, the dominant-negative Jak2
but not the dominant-negative Jak1 suppresses c-fos
promoter activation. To determine whether the chimeric receptor
/ß,ß is functional in vivo, we developed transgenic mice
expressing the chimeric receptor /ß,ß. Bone marrow cells from
the transgenic mice expressing the /ß,ß receptor form not only
GM colonies but also various lineages of colonies in response to
GM-CSF. In addition, mast cells were produced when bone marrow cells of
the transgenic mouse were cultured with hGM-CSF. Thus, it appears that
the cytoplasmic region of the subunit is not required for hGM-CSF
promoting activities, even in bone marrow cells.
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