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(Received for publication, May 21, 1996, and in revised form, September 23, 1996)
From the Related adhesion focal tyrosine kinase (RAFTK),
also known as proline-rich tyrosine kinase 2 and cellular adhesion
kinase
Volume 271, Number 49,
Issue of December 6, 1996
pp. 31222-31226
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
,
Division of Hematologic Malignancies,
Dana-Farber Cancer Institute and Harvard Medical School,
Boston, Massachusetts 02115 and § Division of Hematology
and Oncology, Deaconess Hospital and Harvard Medical School,
Boston, Massachusetts 02115
, has been recently cloned and characterized as a member of
the focal adhesion kinase (FAK) subfamily. RAFTK has an overall 48% amino acid homology to p125FAK and contains a kinase domain
but lacks a transmembrane region, myristylation sites, and Src homology
region 2 and 3 domains. By Northern blot analysis, RAFTK is expressed
in myeloid, lymphoid, and megakaryocytic hematopoietic cells. Like
p125FAK, we found that RAFTK interacts with the focal
adhesion protein paxillin. In the lymphoid cell line BaF3 and the
myeloid cell line 32Dcl3, RAFTK coprecipitates with paxillin. Using
in vitro binding assays, RAFTK and paxillin were shown to
bind directly, through a segment of paxillin that required amino acids
100-227 and a domain in the C terminus of RAFTK. In vitro,
RAFTK could phosphorylate paxillin on tyrosine residues. These results
suggest that RAFTK, as well as p125FAK, may be important in
phosphotyrosine-signaling events within the focal adhesion.
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