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XB-IMG-171171

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Fig. 8. PGAM5-mediated dephosphorylation inhibits nuclear function of DVL2. (A) Endogenous β-Catenin and DVL2 were detected in the cytoplasmic and nuclear fractions from WNT3A stimulated HEK293T cells transfected as indicated. GAPDH, LAMIN-B and pan-Cadherin were used as markers for cytoplasm, nuclei and membrane fractions, respectively. The ratio between the hyperphosphorylated band (a) and the faster migrating band (b) of DVL2 in nuclear and cytoplasmic fractions are plotted in the graph (data are average±s.d. from at least three independent experiments; *P<0.05; n.s., not significant; separate variances t-test). (B) In whole-cell lysates of HEK293T cells, Xenopus Tcf1-Flag co-precipitated with overexpressed Myc-Dvl2 and endogenous β-Catenin irrespective of WNT3A stimulation. Co-expression of Pgam5-HA strongly reduced interaction between Tcf1-Flag, Myc-Dvl2 and endogenous β-Catenin; WNT3A stimulation moderately enhanced interaction of Tcf1 with Dvl2, but not β-Catenin in the presence of exogenous Pgam5. (C) In the inverse co-immunoprecipitation experiment Myc-Dvl2 was immunoprecipitated. The WNT3A-induced interaction of Tcf1-Flag with Myc-Dvl2 was blocked by co-expression of Pgam5.

Image published in: Rauschenberger V et al. (2017)

Copyright © 2017. 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.

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