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Blood, Vol. 94 No. 6 (September 15), 1999:
pp. 1979-1986
Signaling via Src Family Kinases Is Required for Normal
Internalization of the Receptor c-Kit
Virginia C. Broudy,
Nancy L. Lin,
W. Conrad Liles,
Seth J. Corey,
Bridget O'Laughlin,
Sherry Mou, and
Diana Linnekin
From the Divisions of Hematology and Allergy and Infectious Disease,
Department of Medicine, University of Washington, Seattle, WA; the
Division of Hematology-Oncology, Children's Hospital of Pittsburgh,
Pittsburgh, PA; the Intramural Research and Support Program, SAIC
Frederick, National Cancer Institute-Frederick Cancer Research and
Development Center, Frederick, MD; and the Laboratory of Leukocyte
Biology, Division of Basic Sciences, National Cancer
Institute-Frederick Cancer Research and Development Center, Frederick,
MD.
Stem cell factor (SCF) exerts its biological effects by binding to a
specific receptor, the tyrosine kinase c-Kit, which is expressed on the
cell surface. Although normal cellular trafficking of growth factor
receptors may play a critical role in the modulation of receptor
function, the mechanisms that regulate the distribution of c-Kit on the
cell surface and the internalization of c-Kit have not been fully
defined. We investigated whether signal transduction via Src family
kinases is required for normal c-Kit trafficking. Treatment of the
SCF-responsive human hematopoietic cell line MO7e with the inhibitor of
Src family kinases PP1 blocked SCF-induced capping of c-Kit and
internalization of c-Kit. c-Kit was able to associate with clathrin in
the presence of PP1, suggesting that entry of c-Kit into
clathrin-coated pits occurs independently of Src family kinases.
SCF-induced internalization of c-Kit was also diminished in the D33-3
lymphoid cell line in which expression of Lyn kinase was disrupted by
homologous recombination. These results indicate that Src family
kinases play a role in ligand-induced trafficking of c-Kit.
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