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(Received for publication, May 13, 1996, and in revised form, February 6, 1997)
From the Divisions of Experimental Medicine and
Hematology/Oncology, Beth Israel Deaconess Medical Center (West
Campus), Harvard Medical School, Boston, Massachusetts 02215
We have characterized signaling pathways
involving the related adhesion focal tyrosine kinase (RAFTK, also known
as PYK2 or CAK-
Volume 272, Number 16,
Issue of April 18, 1997
pp. 10804-10810
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
) in CMK human megakaryocytic cells. Stem cell
factor, which potentiates the growth of megakaryocytes and their
progenitors, and phorbol myristate acetate, which causes
differentiation of megakaryocytic cell lines, induced the tyrosine
phosphorylation of RAFTK but not of focal adhesion kinase. Stimulation
of CMK cells with stem cell factor resulted in an increase in the
autophosphorylation and kinase activity of RAFTK. Phosphorylation of
RAFTK under these conditions was mediated by a protein kinase
C-dependent pathway. Cytochalasin D, which disrupts the
cytoskeleton, abolished the phosphorylation of RAFTK upon phorbol
myristate acetate and stem cell factor stimulation, indicating that
RAFTK association with the actin cytoskeleton appears to be critical
for its phosphorylation. In addition, we observed an association of
RAFTK with paxillin, a 68-kDa cytoskeleton protein. Using in
vitro binding assays, RAFTK and paxillin were shown to bind
directly through the C-terminal proline-rich domain. Transient
overexpression of a dominant-negative mutant of RAFTK inhibited
significantly the tyrosine phosphorylation of paxillin upon phorbol
myristate acetate stimulation. These observations indicate that RAFTK
might play an important role in the phosphorylation of signaling
pathways within the focal adhesions and that RAFTK participates in
signaling events that link signals from the cell surface to the
cytoskeleton. Furthermore, this study suggests that RAFTK might be
involved in megakaryocyte proliferation and differentiation.
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