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(Received for publication, April 27, 1996, and in revised form, October 15, 1996)
From the Integrin ligation initiates intracellular
signaling events, among which are the activation of protein tyrosine
kinases. The related adhesion focal tyrosine kinase (RAFTK), also known
as PYK2 and CAK
Volume 272, Number 1,
Issue of January 3, 1997
pp. 228-232
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
1-Integrin Stimulation in B Cells
and Binds to p130cas
,
,
,
Division of Hematologic Malignancies,
Dana-Farber Cancer Institute, and § Division of Hematology
and Oncology, Deaconess Hospital, Department of Medicine, Harvard
Medical School, Boston, Massachusetts 02115
, is a tyrosine kinase that is homologous to the focal adhesion kinase (FAK) p125FAK. The structure of RAFTK
is similar to p125FAK in that it lacks a transmembrane
region, does not contain Src homology 2 or 3 domains, and has a
proline-rich region in its C terminus. Here we report that RAFTK is a
target for 1-integrin-mediated tyrosine phosphorylation in both
transformed and normal human B cells. Ligation of the B cell antigen
receptor also induced tyrosine phosphorylation of RAFTK.
Phosphorylation of RAFTK following integrin- or B cell antigen
receptor-mediated stimulation was decreased by prior treatment of cells
with cytochalasin B, indicating that this process was at least
partially cytoskeleton-dependent. One of the
tyrosine-phosphorylated substrates after integrin stimulation in
fibroblasts is p130cas, which can associate with
p125FAK. RAFTK also interacted constitutively with
p130cas in B cells, since p130cas was detected in RAFTK
immunoprecipitates. Although the function of RAFTK remains unknown,
these data suggest that RAFTK may have a significant function in
integrin-mediated signaling pathways in B cells.
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