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Integrins: three is the magic number

The ability of cell surface integrins to link the extracellular matrix (ECM) to the actin cytoskeleton is central to cell motility: if an ECM-anchored integrin is attached to the cytoskeleton, the cytoskeleton can pull on it and so drive the cell forward. Cytoskeletal attachment appears to require integrin clustering, but how big must each cluster be? Harold Erickson and co-workers have approached this question by examining the number of integrin molecules needed to translocate fibronectin-coated beads across the surface of a cell at constant velocity — an assay for cytoskeletal attachment (see p. 2581). They find that beads coated with fibronectin constructs containing three or five cell-adhesion domains, which should produce clusters of three and five integrins, respectively, bind strongly to and translocate across the cell surface. Fibronectin constructs containing one or two adhesion domains (which would form only integrin monomers/dimers) by contrast exhibit only brief binding and random movement. A cluster of at least three integrins thus seems to be required for productive cytoskeletal interactions — which is an interesting contrast to the paradigm of receptor dimerization in signalling.

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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
JCS 2002 115: 2581-2590. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?