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. 2015 Mar 15;26(6):1160–1173. doi: 10.1091/mbc.E14-08-1276

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© 2015 Jin, Chung, 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: — Akt promotes cytoplasmic sequestration of Fam13a and binding between Fam13a and 14-3-3. (A) Representative immunofluorescence images, showing the subcellular distribution of Fam13a when cotransfected with an empty vector or Akt-myr in NIH3T3 cells. (B) Representative immunofluorescence images, showing subcellular localization of Fam13a in NIH3T3 cells treated with DMSO (control), OA, wortmannin, LY294002, OA plus wortmannin, or OA plus LY294002. Fam13a localized in the nucleus in control (DMSO) cells. OA-treated cells exhibited cytoplasmic localization of Fam13a. Fam13a remained in the nucleus in wortmannin, LY294002-, OA/wortmannin-, or OA/LY294002-treated cells. Bar graphs in A and B indicate the percentage of cells that exhibit nuclear, cytoplasmic, or homogeneous subcellular distribution. (C) Inhibition of Akt activation by wortmannin reduces OA-induced binding between Fam13a and 14-3-3 in a GST pull-down assay. Fam13a-expressing NIH3T3 cells were treated with DMSO (control), OA, wortmannin, or OA plus wortmannin. Cell lysates were used in a GST pull-down assay. OA treatment strongly enhanced the binding between Fam13a and GST–14-3-3. This effect of OA treatment was reduced by wortmannin treatment. Wortmannin treatment itself had minimal effect on the binding between Fam13a and GST-14-3-3.