PMID:12867986

Citation	Jiang, G, Giannone, G, Critchley, DR, Fukumoto, E and Sheetz, MP (2003) Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424:334-7
Abstract	Mechanical forces on matrix-integrin-cytoskeleton linkages are crucial for cell viability, morphology and organ function. The production of force depends on the molecular connections from extracellular-matrix-integrin complexes to the cytoskeleton. The minimal matrix complex causing integrin-cytoskeleton connections is a trimer of fibronectin's integrin-binding domain FNIII7-10 (ref. 4). Here we report a specific, molecular slip bond that was broken repeatedly by a force of 2 pN at the cellular loading rate of 60 nm x s(-1); this occurred with single trimer beads but not with monomer. Talin1, which binds to both integrins and actin filaments in vitro, is required for the 2-pN slip bond and rapid cytoskeleton binding. Further, inhibition of fibronectin binding to alpha(v)beta3 and deletion of beta3 markedly decreases the 2-pN force peak. We suggest that talin1 initially forms a molecular slip bond between closely packed fibronectin-integrin complexes and the actin cytoskeleton, which can apply a low level of force to fibronectin until many bonds form or a signal is received to activate a force response.
Links	PubMed Online version:10.1038/nature01805
Keywords	3T3 Cells; Actins/metabolism; Animals; Cell Line; Cytoskeleton/metabolism; Fibronectins/metabolism; Integrin alphaVbeta3/antagonists & inhibitors; Integrin alphaVbeta3/metabolism; Integrin beta3/genetics; Integrin beta3/metabolism; Mice; Protein Binding; Talin/genetics; Talin/metabolism
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