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. 2015 Feb 15;26(4):622–635. doi: 10.1091/mbc.E14-02-0740

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© 2015 Cleghorn et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 8: — Model of the mechanism of focal adhesion disassembly. Focal adhesions are multiprotein complexes organized around clustered active integrins that bind extracellular matrix (shown as fibronectin). FAs are connected to actin filaments and include numerous structural and signaling proteins, such as talin, vinculin, paxillin, focal adhesion kinase (FAK), and so on. FAs are very dynamic, and their disassembly is facilitated by the proximity of microtubules and triggered by clathrin-dependent internalization of integrins. Our data suggest that nonvisual arrestins, known to interact with both microtubules and clathrin, serve as a link between the two, being delivered together with associated clathrin by microtubules to FAs. The delivery of arrestin-bound clathrin to FAs facilitates integrin internalization via clathrin-coated pits (with the help of dynamin, which pinches coated vesicles off of the membrane) and thus FA disassembly.