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β-Arrestin interacts with the beta/gamma subunits of trimeric G-proteins and dishevelled in the Wnt/Ca(2+) pathway in xenopus gastrulation
K. Seitz, V. Dürsch, J. Harnoš, V. Bryja, M. Gentzel, A. Schambony,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
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- MeSH
- Adaptor Proteins, Signal Transducing metabolism MeSH
- Enzyme Activation MeSH
- Arrestins metabolism MeSH
- Embryo, Nonmammalian metabolism MeSH
- Phosphoproteins metabolism MeSH
- Gastrulation * MeSH
- Heterotrimeric GTP-Binding Proteins metabolism MeSH
- Protein Subunits metabolism MeSH
- Protein Kinase C-alpha metabolism MeSH
- Wnt Signaling Pathway MeSH
- Protein Transport MeSH
- Calcium Signaling MeSH
- Protein Binding MeSH
- Xenopus laevis embryology metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
β-Catenin independent, non-canonical Wnt signaling pathways play a major role in the regulation of morphogenetic movements in vertebrates. The term non-canonical Wnt signaling comprises multiple, intracellularly divergent, Wnt-activated and β-Catenin independent signaling cascades including the Wnt/Planar Cell Polarity and the Wnt/Ca(2+) cascades. Wnt/Planar Cell Polarity and Wnt/Ca(2+) pathways share common effector proteins, including the Wnt ligand, Frizzled receptors and Dishevelled, with each other and with additional branches of Wnt signaling. Along with the aforementioned proteins, β-Arrestin has been identified as an essential effector protein in the Wnt/β-Catenin and the Wnt/Planar Cell Polarity pathway. Our results demonstrate that β-Arrestin is required in the Wnt/Ca(2+) signaling cascade upstream of Protein Kinase C (PKC) and Ca(2+)/Calmodulin-dependent Protein Kinase II (CamKII). We have further characterized the role of β-Arrestin in this branch of non-canonical Wnt signaling by knock-down and rescue experiments in Xenopus embryo explants and analyzed protein-protein interactions in 293T cells. Functional interaction of β-Arrestin, the β subunit of trimeric G-proteins and Dishevelled is required to induce PKC activation and membrane translocation. In Xenopus gastrulation, β-Arrestin function in Wnt/Ca(2+) signaling is essential for convergent extension movements. We further show that β-Arrestin physically interacts with the β subunit of trimeric G-proteins and Dishevelled, and that the interaction between β-Arrestin and Dishevelled is promoted by the beta/gamma subunits of trimeric G-proteins, indicating the formation of a multiprotein signaling complex.
Institute of Biophysics Academy of Sciences of the Czech Republic Brno Czech Republic
Institute of Experimental Biology Faculty of Science Masaryk University Brno Czech Republic
Max Planck Institute of Molecular Cell Biology and Genetics Dresden Germany
References provided by Crossref.org
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