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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 3: — Lasp-2 interacts with paxillin. (A) Lasp-2 (green) colocalizes with paxillin (red) at focal adhesions. HEK 293 cells were transfected with GFP–lasp-2 and stained for paxillin. Areas of colocalization are highlighted with arrows. Scale bar, 10 μm. (B) For analysis with the Y2H, yeast strain AH109 was cotransfected with a bait vector coding for lasp-2 and a prey vector coding for paxillin. The binding site for paxillin on lasp-2 was found to be the SH3 domain of lasp-2 using different lasp-2 bait constructs. (C) Paxillin binds to lasp-2 in a saturable manner in ELISA. A 10-pmol amount of GST–lasp-2 or GST alone was immobilized on microtiter plates and incubated with increasing amounts of paxillin. Bound paxillin was detected with an anti-paxillin antibody. (D) Lasp-2 coimmunoprecipitates with paxillin. Endogenous paxillin was immunoprecipitated from HEK 293 cell lysates expressing either GFP or GFP–lasp-2. GFP–lasp–2 coimmunoprecipitated with paxillin.