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. 2013 Apr 1;24(7):995–1006. doi: 10.1091/mbc.E12-10-0723

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© 2013 Bliss 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 5: — The interaction of vinculin and paxillin is enhanced in the presence of lasp-2 and diminished in the presence of lasp-1. Vinculin and paxillin are known binding partners, and the presence of GFP–lasp-2 enhances the amount of paxillin protein that is coimmunoprecipitated with vinculin in HEK 293 lysates when compared with controls. Endogenous vinculin was immunoprecipitated from cell lysates expressing GFP-paxillin and GFP, GFP–lasp-2, Cherry-lasp-1, or GFP–lasp-2 and Cherry–lasp-1 together. GFP-paxillin is more robustly coimmunoprecipitated in lysates with GFP–lasp-2. This enhancement is not detectable when lasp-2 is lost from the complex as a result of Cherry–lasp-1 expression.