schliessen

Filtern

 

Bibliotheken

β-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo

The Wnt/β-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein β-arrestin. Using Dvl deletion constr... Full description

Journal Title: Proceedings of the National Academy of Sciences 17 April 2007, Vol.104(16), p.6690
Main Author: Vítězslav Bryja
Other Authors: Dietmar Gradl , Alexandra Schambony , Ernest Arenas , Gunnar Schulte
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0611356104
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: pnas_s104_16_6690
title: β-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo
format: Article
creator:
  • Vítězslav Bryja
  • Dietmar Gradl
  • Alexandra Schambony
  • Ernest Arenas
  • Gunnar Schulte
subjects:
  • Sciences (General)
ispartof: Proceedings of the National Academy of Sciences, 17 April 2007, Vol.104(16), p.6690
description: The Wnt/β-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein β-arrestin. Using Dvl deletion constructs, we found that β-arrestin binds a region N-terminal of the PDZ domain of Dvl, which contains casein kinase 1 (CK1) phosphorylation sites. Inhibition of Wnt signaling by CK1 inhibitors reduced the binding of β-arrestin to Dvl. Moreover, mouse embryonic fibroblasts lacking β-arrestins were able to phosphorylate LRP6 in response to Wnt-3a but decreased the activation of Dvl and blocked β-catenin signaling. In addition, we found that β-arrestin can bind axin and forms a trimeric complex with axin and Dvl. Furthermore, treatment of Xenopus laevis embryos with β-arrestin morpholinos reduced the activation of endogenous β-catenin, decreased the expression of the β-catenin target gene, Xnr3, and blocked axis duplication induced by X-Wnt-8, CK1ε, or DshΔDEP, but not by β-catenin. Thus, our results identify β-arrestin as a necessary component for Wnt/β-catenin signaling, linking Dvl and axin, and open a vast array of signaling avenues and possibilities for cross-talk with other β-arrestin-dependent signaling pathways. canonical Wnt signaling dishevelled Frizzled G protein-coupled receptor Xenopus
language: eng
source:
identifier: ISSN: 0027-8424 ; E-ISSN: 1091-6490 ; DOI: 10.1073/pnas.0611356104
fulltext: fulltext_linktorsrc
issn:
  • 0027-8424
  • 00278424
  • 1091-6490
  • 10916490
url: Link


@attributes
ID1434041033
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid104_16_6690
sourceidpnas_s
recordidTN_pnas_s104_16_6690
sourcesystemPC
dbid
0PNE
1RNA
pqid201379206
display
typearticle
titleβ-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo
creatorVítězslav Bryja ; Dietmar Gradl ; Alexandra Schambony ; Ernest Arenas ; Gunnar Schulte
ispartofProceedings of the National Academy of Sciences, 17 April 2007, Vol.104(16), p.6690
identifier
subjectSciences (General)
descriptionThe Wnt/β-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein β-arrestin. Using Dvl deletion constructs, we found that β-arrestin binds a region N-terminal of the PDZ domain of Dvl, which contains casein kinase 1 (CK1) phosphorylation sites. Inhibition of Wnt signaling by CK1 inhibitors reduced the binding of β-arrestin to Dvl. Moreover, mouse embryonic fibroblasts lacking β-arrestins were able to phosphorylate LRP6 in response to Wnt-3a but decreased the activation of Dvl and blocked β-catenin signaling. In addition, we found that β-arrestin can bind axin and forms a trimeric complex with axin and Dvl. Furthermore, treatment of Xenopus laevis embryos with β-arrestin morpholinos reduced the activation of endogenous β-catenin, decreased the expression of the β-catenin target gene, Xnr3, and blocked axis duplication induced by X-Wnt-8, CK1ε, or DshΔDEP, but not by β-catenin. Thus, our results identify β-arrestin as a necessary component for Wnt/β-catenin signaling, linking Dvl and axin, and open a vast array of signaling avenues and possibilities for cross-talk with other β-arrestin-dependent signaling pathways. canonical Wnt signaling dishevelled Frizzled G protein-coupled receptor Xenopus
languageeng
source
version6
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
linktorsrc$$Uhttp://www.pnas.org/content/104/16/6690.abstract$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
search
creatorcontrib
0Vítězslav Bryja
1Dietmar Gradl
2Alexandra Schambony
3Ernest Arenas
4Gunnar Schulte
titleβ-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo
description

The Wnt/β-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein β-arrestin. Using Dvl deletion constructs, we found that β-arrestin binds a region N-terminal of the PDZ domain of Dvl, which contains casein kinase 1 (CK1) phosphorylation sites. Inhibition of Wnt signaling by CK1 inhibitors reduced the binding of β-arrestin to Dvl. Moreover, mouse embryonic fibroblasts lacking β-arrestins were able to phosphorylate LRP6 in response to Wnt-3a but decreased the activation of Dvl and blocked β-catenin signaling. In addition, we found that β-arrestin can bind axin and forms a trimeric complex with axin and Dvl. Furthermore, treatment of Xenopus laevis embryos with β-arrestin morpholinos reduced the activation of endogenous β-catenin, decreased the expression of the β-catenin target gene, Xnr3, and blocked axis duplication induced by X-Wnt-8, CK1ε, or DshΔDEP, but not by β-catenin. Thus, our results identify β-arrestin as a necessary component for Wnt/β-catenin signaling, linking Dvl and axin, and open a vast array of signaling avenues and possibilities for cross-talk with other β-arrestin-dependent signaling pathways. canonical Wnt signaling dishevelled Frizzled G protein-coupled receptor Xenopus

subjectSciences (General)
general
0English
1National Acad Sciences
210.1073/pnas.0611356104
3PNAS (National Academy of Sciences)
4National Academy of Sciences (U.S.)
sourceidpnas_s
recordidpnas_s104_16_6690
issn
00027-8424
100278424
21091-6490
310916490
rsrctypearticle
creationdate2007
addtitleProceedings of the National Academy of Sciences
searchscope
0pnas_full
1pnas4
2pnas5
scope
0pnas_full
1pnas4
2pnas5
lsr45$$EView_full_text_in_National_Academy_of_Sciences_(Access_to_full_text_may_be_restricted)
tmp01
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
tmp02
0PNE
1RNA
startdate20070417
enddate20070417
lsr40Proceedings of the National Academy of Sciences, 17 April 2007, Vol.104 (16), p.6690
doi10.1073/pnas.0611356104
citationpf 6690 vol 104 issue 16
lsr30VSR-Enriched:[pqid, pages]
sort
titleβ-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo
authorVítězslav Bryja ; Dietmar Gradl ; Alexandra Schambony ; Ernest Arenas ; Gunnar Schulte
creationdate20070417
lso0120070417
facets
frbrgroupid8327113516446042602
frbrtype5
newrecords20190724
languageeng
topicSciences (General)
collection
0PNAS (National Academy of Sciences)
1National Academy of Sciences (U.S.)
prefilterarticles
rsrctypearticles
creatorcontrib
0Vítězslav Bryja
1Dietmar Gradl
2Alexandra Schambony
3Ernest Arenas
4Gunnar Schulte
jtitleProceedings of the National Academy of Sciences
creationdate2007
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext_linktorsrc
addata
au
0Vítězslav Bryja
1Dietmar Gradl
2Alexandra Schambony
3Ernest Arenas
4Gunnar Schulte
atitleβ-Arrestin is a necessary component of Wnt/β-catenin signaling in vitro and in vivo
jtitleProceedings of the National Academy of Sciences
risdate20070417
volume104
issue16
spage6690
issn0027-8424
eissn1091-6490
formatjournal
genrearticle
ristypeJOUR
abstract

The Wnt/β-catenin signaling pathway is crucial for proper embryonic development and tissue homeostasis. The phosphoprotein dishevelled (Dvl) is an integral part of Wnt signaling and has recently been shown to interact with the multifunctional scaffolding protein β-arrestin. Using Dvl deletion constructs, we found that β-arrestin binds a region N-terminal of the PDZ domain of Dvl, which contains casein kinase 1 (CK1) phosphorylation sites. Inhibition of Wnt signaling by CK1 inhibitors reduced the binding of β-arrestin to Dvl. Moreover, mouse embryonic fibroblasts lacking β-arrestins were able to phosphorylate LRP6 in response to Wnt-3a but decreased the activation of Dvl and blocked β-catenin signaling. In addition, we found that β-arrestin can bind axin and forms a trimeric complex with axin and Dvl. Furthermore, treatment of Xenopus laevis embryos with β-arrestin morpholinos reduced the activation of endogenous β-catenin, decreased the expression of the β-catenin target gene, Xnr3, and blocked axis duplication induced by X-Wnt-8, CK1ε, or DshΔDEP, but not by β-catenin. Thus, our results identify β-arrestin as a necessary component for Wnt/β-catenin signaling, linking Dvl and axin, and open a vast array of signaling avenues and possibilities for cross-talk with other β-arrestin-dependent signaling pathways. canonical Wnt signaling dishevelled Frizzled G protein-coupled receptor Xenopus

pubNational Acad Sciences
doi10.1073/pnas.0611356104
urlhttp://www.pnas.org/content/104/16/6690.abstract
lad01Proceedings of the National Academy of Sciences
pages6690-6695
date2007-04-17