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A more recent version of this article appeared on March 29, 2002
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M110291200v1
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Papers In Press, published online ahead of print January 22, 2002
J. Biol. Chem, 10.1074/jbc.M110291200
Submitted on October 25, 2001
Revised on January 22, 2002
Accepted on January 21, 2002

Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5

Fabienne Denhez, Sarah A. Wilcox-Adelman, Peter C. Baciu, Stefania Saoncella, Sohyung Lee, Becki French, Wendy Neveu, and Paul F. Goetinck

Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown, MA 02129

Corresponding Author: paul.goetinck{at}cbrc2.mgh.harvard.edu

Syndecan-4 and integrins are the primary transmembrane receptors of focal adhesions in cells adherent to extracellular matrix molecules. Syndesmos is a cytoplasmic protein that interacts specifically with the cytoplasmic domain of syndecan-4 and it colocalizes with syndecan-4 in focal contacts. In the present study we sought possible interactors with syndesmos. We find that syndesmos interacts with the focal adhesion adaptor protein paxillin. The binding of syndesmos to paxillin is direct and these interactions are triggered by the activation of protein kinase C. Syndesmos also binds the paxillin homolog, Hic-5. The connection of syndecan-4 with paxillin through syndesmos parallels the connection between paxillin and integrins and may thus reflect the cooperative signaling of these two receptors in the assembly of focal adhesions and actin stress fibers.


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