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Title: Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin.
Authors: Jiang, G
Giannone, G
Critchley, DR
Fukumoto, E
Sheetz, MP
First Published: 17-Jul-2003
Citation: NATURE, 2003, 424 (6946), pp. 334-337
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.
DOI Link: 10.1038/nature01805
eISSN: 1476-4687
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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