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The c-kit-encoded tyrosine kinase receptor for stem
cell factor (Kit/SCFR) is crucial for the development of hematopoietic
cells, melanoblasts, and germ cells. Ligand stimulation of Kit/SCFR
leads to receptor dimerization and autophosphorylation on tyrosine
residues. We recently showed, that protein kinase C (PKC) acts in an
SCF-stimulated negative feedback loop, which controls Kit/SCFR tyrosine
kinase activity and modulates the cellular responses to SCF
(Blume-Jensen, P., Siegbahn, A., Stabel, S., Heldin, C.-H., and
Rönnstrand, L.(1993) EMBO J. 12, 4199-4209). We
present here the identification of the major phosphorylation sites for
PKC in Kit/SCFR. Two serine residues in the kinase insert, Ser-741 and
Ser-746, are PKC-dependent phosphorylation sites in vivo and
account for all phosphorylation by PKC in vitro. Together they
comprise more than 60% of the total SCF-stimulated receptor
phosphorylation in living cells and 85-90% of its phosphorylation
in resting cells. Two additional serine residues, Ser-821 close to the
major tyrosine autophosphorylation site in the kinase domain and
Ser-959 in the carboxyl terminus are SCF-stimulated PKC-dependent
phosphorylation sites. However, they are not phosphorylated directly by
PKC-
Volume 270,
Number 23,
Issue of June 9, pp. 14192-14200, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
in vitro. Both specific receptor tyrosine
autophosphorylation and specific receptor-associated
phosphatidylinositide 3`-kinase activity was increased approximately
2-fold in response to SCF in PAE cells stably expressing
Kit/SCFR(S741A/S746A). Furthermore, the kinase activity of
Kit/SCFR(S741A/S746A) toward an exogenous substrate was increased,
which was reflected as a decreased K and
an increased V
, in accordance with the negative
regulatory role of PKC on Kit/SCFR signaling.
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