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. 2013 Sep 15;24(18):2849–2860. doi: 10.1091/mbc.E13-06-0298

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© 2013 Monteiro 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: — JAM-A regulates Rap2 activity and localization to tight junctions. (A) Rap2 colocalizes with JAM-A (JA) in IECs and (B) in colonic mucosa from human pathology specimens. (A, B) Cells and tissues were pretreated with 0.1% Triton X-100 before fixation. (C) Simultaneous down-regulation of JAM-A (JA) and Rap2c (R2c) in SK-CO15 cells has no additive effect on TER compared to isolated down-regulation of JAM-A (JA) or Rap2c (R2c; n = 3; mean relative resistance with 95% confidence interval). (D) JAM-A (JA)–deficient IECs from two independent JAM-A targets display decreased Rap2 activity compared to control cells (NS), as assessed by Ral-GDS pull down (densitometry calculated as Rap2 pull-down signal over total Rap2 signal, relative to NS control). (E) IECs transiently deficient in afadin (AF) have decreased levels of Rap2 activity compared to control cells (Scr; densitometry calculated as Rap2 pull-down signal over total Rap2 signal, relative to Scr control). (F) Rap2 coimmunoprecipitates with afadin from cell lysates solubilized with a Brij97-based buffer. (G) Incubation of confluent SK-CO15 monolayers with σ1 or σ1_G381A (10 μg/ml) for 1 h leads to decreased Rap2c localization at tight junctions.