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Blood, 1 June 2001, Vol. 97, No. 11, pp. 3662-3664
BRIEF REPORT
Cell proliferation through forced engagement of
c-Kit and Flt-3
Kevin G. Otto,
Liqing Jin,
David M. Spencer, and
C. Anthony Blau
From the Division of Hematology, Department of
Medicine, University of Washington, Seattle; and the Department of
Microbiology and Immunology, Baylor College of Medicine, Houston, TX.
To investigate the potential for functional interactions between
heterologous receptors, the cytoplasmic domains of 2 different receptors (c-Kit and Flt-3) were coexpressed in the
interleukin-3-dependent cell line Ba/F3. The receptor signaling
domains were presented in the context of fusion proteins, with c-Kit
linked to the FK506 binding protein (FKBP12) and Flt-3 linked to the
FRB domain of the FKBP12-rapamycin-associated protein. The fusions
were brought into apposition with the use of chemical inducers of
dimerization (CIDs). Two classes of CID were employed. FK1012 and its
synthetic analogue AP1510 bring together 2 copies of the FKBP12 domain, thereby inducing homodimerization of the c-KitFKBP12
fusion. A second type of CID, rapamycin, brings together one FKBP12
domain and one FRB domain, resulting in heterodimerization of the
c-KitFKBP12 and Flt-3FRB fusions. Ba/F3 cell
growth was promoted not only by FK1012- or AP1510-induced
homodimerization of the c-KitFKBP12 fusion (as reported
previously), but also by rapamycin-induced c-KitFKBP12-Flt-3FRB heterodimerization. These
findings demonstrate the potential for a direct functional interaction
between c-Kit and Flt-3.
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