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. 2011 Apr 15;22(8):1340–1352. doi: 10.1091/mbc.E10-09-0754

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© 2011 Shirai 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: — Characteristics of the binding between RalA and RD-PKCη. (A) Weaker binding of RD-PKCη to RalB than RalA. HA-tagged RalA or RalB was expressed in Cos-7 cells. The lysates were incubated with purified GST-RD or GST and pulled down by glutathione–sepharose 4B. The precipitates were applied to 10% SDS–PAGE followed by immunoblotting using HA or GST antibody. (B) No binding of RD-PKCη to Rho family GTPases. Pull-down assay using HA-tagged cdc42, RhoA, or RalA was performed as described in (A). (C) Effect of GDP-β-S or GTP-γ-S on the binding of GST-RD to FLAG-RalA. The binding assay using purified proteins was performed in the presence of 1 mM GDP-β-S or GTP-γ-S. (D) Binding of GST-RD to active form (G28V) and inactive form (G23V) of Ral A. *, degraded products of GST-RD and GST-ΔC1.