beta-arrestin is a necessary component of Wnt/beta-catenin signaling in vitro and in vivo

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Authors	BRYJA Vítězslav GRADL D. SCHAMBONY A. ARENAS E. SCHULTE G.
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	Faculty of Science
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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