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Vol. 273, Issue 2, 1003-1014, January 9, 1998
Forms a Complex with a New Member,
Hic-5, of Proteins Localized at Focal Adhesions
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From the Departments of Cell adhesion kinase The Hic-5 N-terminal domain directly associated in vitro
with the extreme C-terminal region (residue 801 to the end) of CAK Biochemistry and
¶ Pathology, Department
of Pathology, Sapporo Medical University School of Medicine, South-1,
West-17, Chuo-Ku, Sapporo 060, Japan
(CAK/PYK2) is the
second protein-tyrosine kinase of the focal adhesion kinase subfamily.
We identified a cDNA that encodes a CAK-binding protein. This
cDNA clone encodes the human homologue of Hic-5, the cDNA of
which was cloned in 1994 as transforming growth factor 1- and
hydrogen peroxide-inducible mRNA. We found that Hic-5 exclusively
localized at focal adhesions in a rat fibroblast line, WFB. This
localization of Hic-5 was confirmed in WFB cells expressing Myc-tagged
Hic-5. The amino acid sequence of Hic-5 is highly similar to that of
paxillin in the four LD motifs as well as in the four contiguous LIM
domains.
. CAK was coimmunoprecipitated with Hic-5 from the WFB cell lysate. The coimmunoprecipitation of CAK with Hic-5 was markedly inhibited by the addition of the extreme C-terminal region of CAK.
Coimmunoprecipitation of Hic-5 with CAK, which was shown in COS-7
cells doubly transfected with cDNA constructs of CAK and
Myc-tagged Hic-5, was lost when the CAK amino acid residues 741-903
were deleted. Hic-5 was tyrosine-phosphorylated in Src-transformed 3Y1
cells and in cells treated with pervanadate. Hic-5 associated with
CAK was selectively tyrosine-phosphorylated in WFB cells exposed to
hypertonic osmotic stress. These results indicate that Hic-5 is a
paxillin-related component of focal adhesions and binds to CAK,
implying possible involvement of Hic-5 in the downstream signaling of
CAK.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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