beta-arrestin is a necessary component of Wnt/beta-catenin signaling in vitro and in vivo
| Authors | |
|---|---|
| Year of publication | 2007 |
| Type | Article in Periodical |
| Magazine / Source | Proceedings of the National Academy of Sciences of the U.S.A. |
| MU Faculty or unit | |
| Citation | |
| Field | Genetics and molecular biology |
| Keywords | canonical Wnt signaling; dishevelled; Frizzled |
| Description | The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein beta-arrestin. MEFs lacking beta-arrestins were able to phosphorylate Lrp6 in response to Wnt-3a, but decreased the activation of Dvl and blocked beta-catenin signaling. Furthermore, treatment of Xenopus laevis embryos with beta-arrestin morpholinos reduced the activation of endogenous beta-catenin, decreased the expression of the beta-catenin target gene, Xnr3, and blocked axis duplication induced by X-Wnt-8, and other molecules. Thus, our results identify beta-arrestin as a necessary component for Wnt/ beta-catenin signaling. |
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