| First Author | Jiang G | Year | 2003 |
| Journal | Nature | Volume | 424 |
| Issue | 6946 | Pages | 334-7 |
| PubMed ID | 12867986 | Mgi Jnum | J:84472 |
| Mgi Id | MGI:2667760 | Doi | 10.1038/nature01805 |
| Citation | Jiang G, et al. (2003) Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424(6946):334-7 |
| abstractText | 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. |
