Upon Wnt stimulation, Rac1 activation 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

RhoH participates in a multi-protein complex with the zinc finger protein kaiso that regulates both cytoskeletal structures and chemokine-induced T cells

“…After induction of WNT signaling, p120 catenin dissociates from E-cadherin and recruits Kaiso into the nucleus 23 and activates Rac via Vav2. 25 Our results showing RhoH and Kaiso association and both cytosolic and nuclear co-localization in Jurkat cells after chemokine stimulation suggest that RhoH may form a complex with Kaiso and p120 catenin. To investigate this possibility, we determined the association of RhoH with p120 catenin in Jurkat cells.…”

Mib1 contributes to persistent directional cell migration by regulating the Ctnnd1-Rac1 pathway

“…One possibility is that K547 ubiquitination interferes with the interaction between Ctnnd1 and Vav2. Vav2 is the GEF that promotes GTP binding to Rac1 (40,41), and interaction of Ctnnd1 with Vav2 promotes Rac1 activation (31,42). Therefore, Mib1-driven Ctnnd1 ubiquitination might inhibit the interaction of Ctnnd1 with Vav2, thereby reducing Rac1 activation.…”

“…Excessive atoh1a reduces fgfr1 expression and attenuates FGF signaling in the pLLP, resulting in the expansion of Wnt signal (21). Recently, Valls et al (42) showed that Wnt signal induces Rac1 activity via Ctnnd1 in HEK-293 cells, SW-480 cells, and Xenopus embryos. Therefore, in mib1 ta52b pLLP, the Rac1 activity level might be highly elevated owing to loss of Notchdependent signal in addition to the Mib1-Ctnnd1-Rac1 pathway.…”

Phosphorylation of serine residuesS252,S268/S269, andS879in p120 catenin activates migration of presomitic mesoderm in gastrulating zebrafish embryos

“…5 Dephosphorylation of tyrosine residues 112 or 217 of p120 catenin augments cell migration during convergent extension in Xenopus. 15 In the preceding paper, we show that dephosphorylation of tyrosine residues 217 and 228 of p120 catenin-δ1-3A (CTNND1-3A) accomplishes the same in zebrafish embryos. 16 In cell cultures, the phosphorylation of p120 catenin is known to occur on six serine (S) and two threonine (T) residues in the N-and C-terminal regions, which include S122, S252, S268, S288, T310, S312, S879, and T916.…”