Wnt controls the transcriptional activity of Kaiso through CK1ε-dependent phosphorylation of p120-catenin

Abstract

There was an error published in J. Cell Sci. 124, 2298-2309.Some of the blots presented in Fig. 4A were inadvertently duplicated in Fig. 6D. The blots in Fig. 4A are correct as presented. The correct Fig. 6 is presented below. There are no changes to the figure legend, which is accurate. This error does not affect the conclusions of the study.The authors apologise to the readers for any confusion that this error might have caused. . Kaiso also interacts with β-catenin and its binding is regulated by p120-catenin. (A) 2 pmol of recombinant GST-Kaiso or GST as a control was incubated with 1 pmol of full-length β-catenin or two deletion mutants comprising armadillo repeats 1-12 (amino acids 120-683) or 1-6 (amino acids 120-420). Protein complexes were affinity purified with glutathione-Sepharose and analyzed by western blotting (WB) with anti-β-catenin antibody. Blots were re-analyzed with anti-GST antibody to ensure that a similar amount of fusion protein was present. (B) 2 pmol of recombinant GST-Kaiso, or GST as a control, was incubated with 2 pmol of p120-catenin (amino acids 102-911) (left-hand panel) or 2 pmol of full-length β-catenin (right-hand panel). Protein complexes were affinity purified with glutathione-Sepharose and analyzed by western blotting with the indicated antibodies. 'St' indicates the signal obtained with known amounts of recombinant proteins used as control. (C) Pull-down assays were performed by incubating 7 pmol of GST-Kaiso with 400 μg of whole-cell extracts from SW-480 cells transfected with pcDNA3-Tcf-4-HA. When indicated, 35 pmols of p120-catenin or β-catenin was added to the incubation medium. Protein complexes were affinity purified and analyzed by western blotting with the indicated antibodies. (D) SW-480 cells were infected with scrambled shRNA (Ctl) or shRNA specific for p120-catenin, and were treated with control or Wnt3a-conditioned medium for 6 hours. Kaiso was immunoprecipitated (IP) and immunocomplexes were analyzed by western blotting. (E) SW480 cells were treated with control or Wnt3a-conditioned medium for 6 hours. β-catenin was immunoprecipitated from SW-480 total cell extracts and the immunocomplex was analyzed by western blotting. In the input lane, 5% of each total cell extract used is shown. (F) Kaiso was immunoprecipitated with a specific antibody from total cell extracts of HT29-M6 cells treated with control or Wnt3a-conditioned medium for 6 hours. Associated proteins were analyzed by western blotting. All the data presented in this figure are representative of at least three independent experiments. Irr IgG, an irrelevant IgG used as control in the immunoprecipitation. 873

The contribution of TGF-β in Epithelial–Mesenchymal Transition (EMT): Down-regulation of E-cadherin via snail

“…The β-catenin signaling is activated by the loss of E-cadherin-induced EMT. The activation of β-catenin downstream depends on the association of the Wnt co-receptor and the E-cadherin/catenin complex [64]. The translocation and accumulation of β-catenin into nucleus followed the progressive loss of E-cadherin and acquisition of mesenchymal markers such as Fibronectin [65].…”

Novel truncating mutations inCTNND1cause a dominant craniofacial and cardiac syndrome

“…The protein has a second function as a scaffolding 71 protein for the GTPase RhoA and associated Rho regulatory proteins 18,19 . In addition, it can also 72 directly interact with the zinc finger transcriptional repressor Kaiso (ZBTB33), facilitating Wnt signal 73 transduction 20,21 . Thus, p120-catenin appears to be a multi-functional protein, promoting epithelial 74 stability when in complex with E-cadherin, and regulating RhoA and transcriptional activities.…”

Cell trajectory modeling identifies a primitive trophoblast state defined by BCAM enrichment

“…Included in this list are TFs known to be important in CTB biology like TEAD4 and TFAP2A 25 . Interestingly, TFs such as transcriptional regulator KAISO ( ZBTB33 ) involved the negative regulation of the WNT pathway 26 shows enrichment in CTB3. These findings highlight the cellular and molecular complexity within the CTB compartment of the placenta, and identify possible transcriptional regulators important in controlling the maintenance of progenitor CTBs as well as regulating the possible transition between unique CTB states.…”