BRYJA, Vítězslav, D. GRADL, A. SCHAMBONY, E. ARENAS and G. SCHULTE. beta-arrestin is a necessary component of Wnt/beta-catenin signaling in vitro and in vivo. Proceedings of the National Academy of Sciences of the U.S.A. 2007, vol. 104, No 16, p. 6690-6695. ISSN 1091-6490.
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Basic information
Original name beta-arrestin is a necessary component of Wnt/beta-catenin signaling in vitro and in vivo
Name in Czech beta-arrestin je nezbytnou složkou Wnt/beta-kateninového signálování jak in vitro, tak in vivo
Authors BRYJA, Vítězslav (203 Czech Republic, guarantor), D. GRADL (276 Germany), A. SCHAMBONY (276 Germany), E. ARENAS (724 Spain) and G. SCHULTE (276 Germany).
Edition Proceedings of the National Academy of Sciences of the U.S.A. 2007, 1091-6490.
Other information
Original language English
Type of outcome Article in a journal
Field of Study Genetics and molecular biology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
RIV identification code RIV/00216224:14310/07:00025662
Organization unit Faculty of Science
UT WoS 000245869200037
Keywords in English canonical Wnt signaling; dishevelled; Frizzled
Tags canonical Wnt signaling, Dishevelled, Frizzled
Tags International impact
Changed by Changed by: prof. Mgr. Vítězslav Bryja, Ph.D., učo 11088. Changed: 8/7/2009 10:37.
Abstract
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.
Abstract (in Czech)
Fosfoprotein dishevelled (Dvl), který je integrální součástí Wnt dráhy fyzicky interaguje s multifunkčním proteinem beta-arrestinem. MEF buňky, které nemají beta-arrestiny jsou sice schopné po přidání Wnt-3a fosforylace proteinu Lrp6 v membráně, ale vykazují sníženou aktivaci Dvl and žádnou aktivaci beta-cateninu. Navíc deplece beta-arrestinu v emryích žab Xenopus laevis snižuje aktivaci endogenního beta-cateninu, expresi Xnr3 a blokuje zdvojení tělní osy, která je indukována X-Wnt8 i jinými aktivátory beta-catenin dráhy. Naše výsledky tak identifikují beta-arrestin jako nezbytnou součást Wnt/beta-catenin dráhy in vitro a in vivo.
Links
MSM0021622430, plan (intention)Name: Funkční a molekulární charakteristiky nádorových a normálních kmenových buněk - identifikace cílů pro nová terapeutika a terapeutické strategie
Investor: Ministry of Education, Youth and Sports of the CR, Functional and molecular characteristics of cancer and normal stem cells - identification of targets for novel therapeutics and therapeutic strategies
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