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Originally published In Press as doi:10.1074/jbc.M605553200 on August 25, 2006

J. Biol. Chem., Vol. 281, Issue 43, 32156-32163, October 27, 2006
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A Conserved NXIP Motif Is Required for Cell Adhesion Properties of the Syndecan-4 Ectodomain*Formula

James R. Whiteford and John R. Couchman1

From the Biomedical Sciences Division, Faculty of Natural Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, London SW7 2AZ, United Kingdom

Syndecans are cell surface proteoglycans involved in cell adhesion and motility. Syndecan-4 is an important component of focal adhesions and is involved in cytoskeletal reorganization. Previous work has shown that the syndecan-4 ectodomain can support cell attachment. Here, three vertebrate syndecan-4 ectodomains were compared, including that of the zebrafish, and we have demonstrated that the cell binding activity of the syndecan-4 ectodomain is conserved. Cell adhesion to the syndecan-4 ectodomain appears to be a characteristic of mesenchymal cells. Comparison of syndecan-4 ectodomain sequences led to the identification of three conserved regions of sequence, of which the NXIP motif is important for cell binding activity. We have shown that cell adhesion to the syndecan-4 ectodomain involves beta1 integrins in several cell types.


Received for publication, June 9, 2006 , and in revised form, August 11, 2006.

* This work was supported 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. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

1 To whom correspondence should be addressed: Biomedical Sciences Div., Faculty of Natural Sciences, Imperial College London, Sir Alexander Fleming Bldg., Exhibition Rd., London SW7 2AZ, UK. Tel.: 44-2075943190; E-mail: j.couchman{at}imperial.ac.uk.


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[Abstract] [Full Text] [PDF]




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