Focal adhesion size controls tension-dependent recruitment of [alpha]-smooth muscle actin to stress fibers

Expression of [alpha]-smooth muscle actin ([alpha]-SMA) renders fibroblasts highly contractile and hallmarks myofibroblast differentiation. We identify [alpha]-SMA as a mechanosensitive protein that is recruited to stress fibers under high tension. Generation of this threshold tension requires the a...

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Bibliographic Details
Published in:The Journal of cell biology 2006, Vol.172 (2), p.259-268
Main Authors: Goffin, Jérôme M, Pittet, Philippe, Csucs, Gabor, Lussi, Jost W, Meister, Jean-Jacques, Hinz, Boris
Format: Article
Language:English
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Summary:Expression of [alpha]-smooth muscle actin ([alpha]-SMA) renders fibroblasts highly contractile and hallmarks myofibroblast differentiation. We identify [alpha]-SMA as a mechanosensitive protein that is recruited to stress fibers under high tension. Generation of this threshold tension requires the anchoring of stress fibers at sites of 8-30-[micro]m-long "supermature" focal adhesions (suFAs), which exert a stress approximately fourfold higher ([approximately]12 nN/[micro]m²) on micropatterned deformable substrates than 2-6-[micro]m-long classical FAs. Inhibition of suFA formation by growing myofibroblasts on substrates with a compliance of
ISSN:0021-9525
1540-8140