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Cited by 934

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Wnt Induces LRP6 Signalosomes and Promotes Dishevelled-Dependent LRP6 Phosphorylation

Bilić, Josipa, Huang, Ya-Lin, Davidson, Gary, Zimmermann, Timo, Cruciat, Cristina-Maria, Bienz, Mariann, Niehrs, Christof·2007·Science

Abstract

Multiple signaling pathways, including Wnt signaling, participate in animal development, stem cell biology, and human cancer. Although many components of the Wnt pathway have been identified, unresolved questions remain as to the mechanism by which Wnt binding to its receptors Frizzled and Low-density lipoprotein receptor–related protein 6 (LRP6) triggers downstream signaling events. With live imaging of vertebrate cells, we show that Wnt treatment quickly induces plasma membrane–associated LRP6 aggregates. LRP6 aggregates are phosphorylated and can be detergent-solubilized as ribosome-sized multiprotein complexes. Phospho-LRP6 aggregates contain Wnt-pathway components but no common vesicular traffic markers except caveolin. The scaffold protein Dishevelled (Dvl) is required for LRP6 phosphorylation and aggregation. We propose that Wnts induce coclustering of receptors and Dvl in LRP6-signalosomes, which in turn triggers LRP6 phosphorylation to promote Axin recruitment and β-catenin stabilization.

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Metadata

Authors
Bilić, J., Huang, Y.-L., Davidson, G., Zimmermann, T., Cruciat, C.-M., Bienz, M., & Niehrs, C.
Venue
Science
Published
2007-06-15
Volume
316
Issue
5831
Pages
1619-1622
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2065431388
Cited by
934
References
7
FWCI
17.00
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Wnt Induces LRP6 Signalosomes and Promotes Dishevelled-Dependent LRP6 Phosphorylation. https://app.cochat.ai/papers/10.1126/science.1137065
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Bilić, J., Huang, Y.-L., Davidson, G., Zimmermann, T., Cruciat, C.-M., Bienz, M., & Niehrs, C. (2007). Wnt Induces LRP6 Signalosomes and Promotes Dishevelled-Dependent LRP6 Phosphorylation. Science. https://doi.org/10.1126/science.1137065

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