Xenbase Image ID: 83464

Figure 3. RAB8B Is Activated by Wnt Ligands and Relocalized by Dvl1 to Promote LRP6 Activity (A) In the Wnt reporter assay, LRP6 synergized with coexpression of constitutively active mutant (c.a., Q67L), whereas dominant-negative mutant (d.n., T22N) had an inhibitory affect (HEK 293T). (B) In the same assay, RAB8B-WT synergized with LRP6 only in the presence of recombinant Wnt3a in HEK 293T (n.s., not significant). (C) RAB8B-WT expression increased active LRP6 and β-catenin levels in the presence of recombinant Wnt3a after 2 hr in HEK 293T. (D) Dvl1 coexpression recruited RAB8B in Dvl1 puncta (HeLa). (E) RAB8B interaction with its activator RABIN8 is stimulated by adding recombinant Wnt3a (normalized to nonspecific band; RFI. relative fluorescence intensity) in HEK 293T. (F and G) RAB8B-WT coimmunoprecipitated with endogenous LRP6 (HEK 293T; b.c., bead control; i.c., isotype control), and both proteins colocalized at the plasma membrane that was further promoted by adding recombinant Wnt3a (1 hr) (PC, Pearson�s coefficient) (HeLa). Error bars represent �SD of three replicates. See also Figures S3 and S4. Image published in: Demir K et al. (2013) Copyright © 2013. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View

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