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J. Biol. Chem., Vol. 278, Issue 47, 46607-46615, November 21, 2003

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Syndecan-1 Transmembrane and Extracellular Domains Have Unique and Distinct Roles in Cell Spreading^*

Kyle J. McQuade and Alan C. Rapraeger

From the Department of Pathology and Laboratory Medicine and Graduate Program in Cellular and Molecular Biology, University of Wisconsin-Madison, Madison, Wisconsin 53706

Raji cells expressing syndecan-1 (Raji-S1) adhere and spread when plated on heparan sulfate-binding extracellular matrix ligands or monoclonal antibody 281.2, an antibody directed against the syndecan-1 extracellular domain. Cells plated on monoclonal antibody 281.2 initially extend a broad lamellipodium, a response accompanied by membrane ruffling at the cell margin. Membrane ruffling then becomes polarized, leading to an elongated cell morphology. Previous work demonstrated that the syndecan-1 cytoplasmic domain is not required for these activities, suggesting important roles for the syndecan-1 transmembrane and/or extracellular domains in the assembly of a signaling complex necessary for spreading. Work described here demonstrates that truncation of the syndecan-1 extracellular domain does not affect the initial lamellipodial extension in the Raji-S1 cells but does inhibit the active membrane ruffling that is necessary for cell polarization. Replacement of the entire syndecan-1 transmembrane domain with leucine residues completely blocks the cell spreading. These data demonstrate that the syndecan-1 transmembrane and extracellular domains have important but distinct roles in Raji-S1 cell spreading; the extracellular domain mediates an interaction that is necessary for dynamic cytoskeletal rearrangements whereas an interaction of the transmembrane domain is required for the initial spreading response.

Received for publication, May 7, 2003 , and in revised form, August 19, 2003.

^* This work was supported by Grant R01-HD21881 from the National Institutes of Health. 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.

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

To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, University of Wisconsin-Madison, 1300 University Ave., Madison, WI 53706. Tel.: 608-262-7577; Fax: 608-265-3301; E-mail: acraprae{at}wisc.edu.

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