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. 2012 May 15;23(10):1846–1859. doi: 10.1091/mbc.E11-12-1057

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© 2012 Hoffman 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 7: — Actin stress fibers formed without VASP recruitment exhibit enhanced sensitivity to actin inhibitor jasplakinolide (Jas). (A, B) In comparison to controls, WT cells treated with jasplakinolide (100 nM, 2 h) accumulated stress fibers and aggregates of F-actin (phalloidin) visible by fluorescence microscopy. F-Actin (phalloidin; C) and zyxin (D) colocalized within the jasplakinolide-induced aggregates. Zyxin (E) and binding partner Mena/VASP (F) also colocalized at the jasplakinolide-induced aggregates. Jasplakinolide treatment (100 nM, 2 h) of zyxin-null cells expressing either GFP- zyx^{F71,93,105,115A} mutant (G) or GFP-zyxin (H) induced a more pronounced actin phenotype, with disruption of zyxin-Mena/VASP interaction (zyx^{F71,93,105,115A}). (I) Time-lapse microscopy of GFP-zyxin in cells (0, 30, 60, 90, and 114 min after 200 nM jasplakinolide addition) showed mobilization from focal adhesions to actin stress fibers, followed by rupture of fiber and accumulation of aggregates (J, arrows; 99, 102, 105 min). See Supplemental Video S1.