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. 2017 Apr 26;292(24):10026–10034. doi: 10.1074/jbc.M117.778233

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© 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 5. — PPP1R3B and PPP1R13L associate with Gwl. A, MBP-PPP1R3B and MBP-PPP1R13L were expressed and purified as described under “Experimental Procedures.” The purified proteins were examined by Coomassie staining. B, MBP-PPP1R3B and MBP-PPP1R13L were purified and bound to amylose resin as in A. Beads were incubated in interphase extract for 30 min and then reisolated. The input and pulldown products were analyzed by immunoblotting for Gwl and PP1γ. C, GST-Gwl pulldown (PD) was performed in interphase extracts with or without supplementation of purified MBP-PPP1R3B and MBP-PPP1R13L. The input and pulldown products were analyzed by immunoblotting for Gwl and PP1γ. Ctr, control. D, Gwl IP was performed in interphase extracts with or without supplementation of purified MBP-PPP1R3B and MBP-PPP1R13L. The input and IP products were analyzed by immunoblotting for Gwl, PP1γ, and MBP. E, MBP-PPP1R3B was purified on beads, incubated with purified GST-Gwl, and reisolated. The input GST-Gwl protein, control pulldown, and MBP pulldown samples were analyzed by immunoblotting for GST and MBP. F, MBP-PPP1R3B pulldown was performed in CSF (M phase, M) or interphase (I) egg extracts. The input and pulldown products were analyzed by immunoblotting for Gwl, PP1γ, and MBP. The data in this figure are representative of three or more independent experiments.