Rac1 activation upon Wnt stimulation requires Rac1 and Vav2 binding to p120-catenin

Abstract

There was an error published in J. Cell Sci. 125, 5288-5301.In Fig. 2B, panels labelled as the actin input and p120-catenin IP:p120-catenin panels were inadvertently assembled to show the same blots. Concerns were also raised about possible duplications and/or splices in Figs 4A, 4E, 5D, 6A and 6C. The authors were unable to obtain the original data in order to address these concerns and therefore repeated the experiments. The new data are shown in the figures below and have been verified by the corresponding author's institute as supporting the original conclusions of the study. There are no changes to the figure legends, which are accurate.The authors acknowledge the increased contribution of Beatriz Del Valle-Pérez in repeating the experiments and apologise to the readers for any confusion that these errors might have caused. Fig. 2. Wnt-induced Rac1 activation is dependent on Vav2 interaction with p120-catenin. Vav2 (A) and p120-catenin (B) were immunoprecipitated from 500 µg SW-480 whole-cell extracts treated with control or Wnt3a-conditioned medium for the times indicated. Protein complexes were analyzed by western blot (WB) with anti-p120-catenin, anti-Vav2, anti-E-cadherin and anti-Rac1. 10 µg of SW-480 whole-cell extracts were included as internal reference (input). The graphs on the right are autoradiograms from four different experiments that were quantified and the mean ± s.d. obtained after 2 hours of incubation with Wnt3a medium. Each value is presented relative to that obtained in cells treated with control medium and normalized with respect to the amount of immunoprecipitated Vav2 or p120-catenin. (C) SW-480 cells stably expressing scrambled or shRNA specific for Vav2 were treated with control or Wnt3a-conditioned medium for 2 hours. GST-PAK pull-down assays were performed and active Rac1 was determined by WB. Autoradiograms from five different experiments performed in triplicate were quantified and the mean ± s.d. was obtained for each condition. Each value is presented relative to that obtained in nondepleted cells treated with control medium. (D) Cytosolic and nuclear lysates were obtained from control and Vav2-depleted SW-480 cells treated with control or Wnt3a-conditioned medium for 15 hours. β-catenin distribution between the two cell compartments was analyzed by WB. 2120© 2016. Published by The Company of Biologists Ltd | Journal of Cell Science (2016Science ( ) 129, 2120Science ( -2123Science ( doi:10.1242 Journal of Cell Science 480 (E,F) cells overexpressing either GFP-p120-catenin wt isoform 1, GFP-p120-catenin point mutants Y112E or Y217E or the empty vector phrGFP, treated when indicated with Wnt3a-conditioned medium for 15 hours. The nuclear fraction was separated from the cytosolic and membrane-associated fraction as detailed in Materials and Methods. β-catenin levels in each cellular fraction were analyzed by WB. Lamin-β1 was used as a nuclear marker and pyruvate kinase as a marker for the cytosolic-plus-membrane fraction. In the right panel of C, p120-catenin wt, Y112E and Y217E...

Defining functional interactions during biogenesis of epithelial junctions

“…These results indicate that VAV2 appears to be upstream of TRIP10 in junction regulation. VAV2 has been shown to interact specifically with the cytoplasmic pools of p120 CTN and β-catenin365152. In contrast, in keratinocytes VAV2 interacts with E-cadherin tail at steady state and during junction assembly.…”

Brazilein in Combination with Cisplatin Inhibit Proliferation and Migration on Highly Metastatic Cancer Cells, 4T1

“…Flavonoid wogonin inhibits Rac1 expression as well as other Ras and activated ERK and PI3K/Akt pathway (Zhao et al, 2014). Upregulation of Rac1 activity is mediated through several signaling pathways including Wnt stimulation that involving binding of p120catenin with Rac1 and Vav2 (Valls et al, 2012). However, our finding (Fig.…”

“…This event mainly induce by the expression and activation of Rac1 and p120 (Valls et al, 2012). On the other hand, cancer progression is also marked by highly expression of proteinases in the microenvironment such as MMP9 to impair ECM (Hua et al, 2011).…”

RhoGTPases, actomyosin signaling and regulation of the Epithelial Apical Junctional Complex

“…In AJs RhoGEF2, RFG and Trio Rho GEF [37-39] bind to E cadherin while Vav2 GEF associates with Nectin and p120 catenin to regulate AJ formation in kidney epithelia [40, 41]. Ect2 serves as a GEF for Cdc42 and RhoA, and it has been shown to stabilize E-cadherin in a complex with the Centralspindlin complex [42].…”