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Trimers of the fibronectin cell adhesion domain localize to actin filament bundles and undergo rearward translocation

Françoise Coussen^*, Daniel Choquet^*, Michael P. Sheetz and Harold P. Erickson^,

Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710, USA
^* Present address UMR CNRS 5091, Université de Bordeaux 2, Institut François Magendie, 33077 Bordeaux, France
Present address: Department of Biological Sciences, Columbia University, New York, NY 10027, USA

Author for correspondence (e-mail: h.erickson{at}cellbio.duke.edu )

Accepted 8 April 2002

Previous studies have shown that small beads coated with FN7-10, a four-domain cell adhesion fragment of fibronectin, bind to cell surfaces and translocate rearward. Here we investigate whether soluble constructs containing two to five FN7-10 units might be sufficient for activity. We have produced a monomer, three forms of dimers, a trimer and a pentamer of FN7-10, on the end of spacer arms. These oligomers could bind small clusters of up to five integrins. Fluorescence microscopy showed that the trimer and pentamer bound strongly to the cell surface, and within 5 minutes were prominently localized to actin fiber bundles. Monomers and dimers showed only diffuse localization. Beads coated with a low concentration (probably one complex per bead) of trimer or pentamer showed prolonged binding and rearward translocation, presumably with the translocating actin cytskeleton. Beads containing monomer or dimer showed only brief binding and diffusive movements. We conclude that clusters of three integrin-binding ligands are necessary and sufficient for coupling to and translocating with the actin cytoskeleton.

Key words: Fibronectin, Cell adhesion, Signalling, Multivalent, Dimerization, Oligomer

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Integrins: three is the magic number

JCS 2002 115: 1203. [Full Text]  

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