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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 6: — Ser-322 is important for subcellular distribution of Fam13a and its interaction with 14-3-3. (A) Representative immunofluorescence images, showing the subcellular distribution of Fam13a and S322A in NIH3T3 cells treated with DMSO (control) or OA. Bar graph indicates the percentage of cells that exhibit nuclear, cytoplasmic, or homogeneous subcellular distribution. (B) A GST pull down, showing that Ser-322 is important for the binding between Fam13a and 14-3-3 and the effect of OA on this interaction. Fam13a- and S322A-expressing NIH3T3 cells were treated with DMSO (control) or OA. Cell lysates were used in a GST pull-down assay. Interaction between Fam13a and 14-3-3 was markedly enhanced in OA-treated cells. In contrast, S322A mutant showed weaker interaction with 14-3-3 in OA-treated cells. (C) Western blot, showing the specificity of the anti-phosphoS322 (pS322) antibody. Note that the anti-pS322 antibody strongly reacted with Fam13a. It did not react with Δ315–329 but recognized S322A weakly. (D) Western blot, showing Ser-322 phosphorylation in NIH3T3 cells treated with DMSO (control), OA, wortmannin, or OA plus wortmannin. pS322 level was increased by OA treatment. The effect of OA on pS322 was reduced by wortmannin treatment. (E) Western blot, showing that overexpression of B56β, B56γ, B56δ, and B56ε decreased Ser-322 phosphorylation. All B56 expression constructs were FLAG tagged.