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J. Biol. Chem., Vol. 278, Issue 16, 13795-13802, April 18, 2003
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From the Syndecan-4 is a transmembrane heparan sulfate
proteoglycan that acts as a coreceptor with integrins in focal adhesion
formation. The central region of syndecan-4 cytoplasmic domain (4V;
LGKKPIYKK) binds phosphatidylinositol 4,5-bisphosphate, and together
they regulate protein kinase C
Direct Binding of Syndecan-4 Cytoplasmic Domain to the
Catalytic Domain of Protein Kinase C
(PKC) Increases Focal
Adhesion Localization of PKC*
,
Department of Cell Biology,
University of Alabama at Birmingham, Alabama 35294, § Schering-Plough Research Institute, Union, New Jersey
07083, and the ¶ Division of Biomedical Sciences, Imperial
College London, London SW7 2AZ, United Kingdom
(PKC) activity. Syndecan 4V
peptide directly potentiates PKC activity, leading to
"superactivation" of the enzyme, apparently through an interaction
with its catalytic domain. We now have performed yeast two-hybrid and
in vitro binding assays to determine the interaction sites
between 4V and PKC. Full-length PKC weakly interacted with 4V by
yeast two-hybrid assays, but PKC constructs that lack the
pseudosubstrate region or constructs of the whole catalytic domain
interacted more strongly. A mutated 4V sequence (4V(YF):
LGKKPIFKK) did not interact with PKC, indicating that tyrosine 192 in the syndecan-4 cytoplasmic domain might be critical for this
interaction. Further assays identified a novel interaction site in the
C terminus of the catalytic domain of PKC (amino acid sequence
513-672). This encompasses the autophosphorylation sites, which
are implicated in activation and stability. Yeast two-hybrid data were
confirmed by in vitro binding and coimmunoprecipitation
assays. The interaction of syndecan-4 with PKC appears unique since
PKC
and 
did not interact with 4V in yeast two-hybrid assays or
coimmunoprecipitate with syndecan-4. Finally, overexpression of
syndecan-4 in rat embryo fibroblast cells, but not expression of the YF
mutant, increased PKC localization to focal adhesions. The data
support a mechanism where syndecan-4 binds PKC and localizes it to
focal adhesions, whose assembly may be regulated by the kinase.
*
This work was supported by National Institutes of Health
Grant GM50194 (to A. W.) and Sankyo Co., Ltd. Additional support was
provided by Wellcome Trust Program Grant 065940 (to J. R. C.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell
Biology, University of Alabama at Birmingham, THT 946, 1530 3rd Ave.
S., Birmingham, AL 35294-0006; Tel.: 205-934-1548; Fax: 205-934-7029; E-mail: anwoods@uab.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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