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Granulocyte-macrophage colony-stimulating factor and interleukin-3 induce
rapid phosphorylation and activation of the proto-oncogene Raf-1 in a human
factor-dependent myeloid cell line
Y Kanakura, B Druker, KW Wood, HJ Mamon, K Okuda, TM Roberts and JD Griffin
Dana-Farber Cancer Institute, Boston, MA 02115.
The product of the c-raf-1 proto-oncogene, Raf-1, is a 74,000-dalton
cytoplasmic serine/threonine protein kinase that has been implicated as an
intermediate in signal transduction mechanisms. In the human factor-
dependent myeloid cell line MO7, both granulocyte-macrophage colony
stimulating factor (GM-CSF) and interleukin-3 (IL-3) were found to induce
rapid, dose-dependent phosphorylation of Raf-1, which resulted in altered
Raf-1 mobility in sodium dodecyl sulfate-polyacrylamide gels. The increase
in phosphorylation was due primarily to an increase in phosphoserine, with
only a minor component (less than 2%) of phosphotyrosine. PMA (12-phorbol
13-myristic acid) also induced Raf-1 phosphorylation in MO7 cells, but the
resulting alteration in electrophoretic mobility was different than that
observed after GM-CSF or IL-3. GM-CSF and IL-3 rapidly and transiently
increased Raf-1 kinase activity using Histone H1 as a substrate in an
immune complex kinase assay in vitro. These results suggest that
phosphorylation of Raf-1 could play a role in some aspect of GM-CSF and
IL-3 signal transduction.
Volume 77,
Issue 2,
pp. 243-248,
01/15/1991
Copyright © 1991 by The American Society of Hematology
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