Evidence map›Paper›PMID 23579495›Full record

ArticleScience (New York, N.Y.)2013

Wnt stabilization of β-catenin reveals principles for morphogen receptor-scaffold assemblies.

Sung-Eun Kim, He Huang, Ming Zhao, Xinjun Zhang, Aili Zhang, Mikhail V Semonov, Bryan T MacDonald, Xiaowu Zhang, Jose Garcia Abreu, Leilei Peng and 1 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed
11.5field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

147 citing papers in PubMed, 236 citations in OpenAlex.

  1. Review
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  8. Article
  9. Article
  10. Review
  11. Geographic and Viral Etiology Patterns ofInternational journal of molecular sciences · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Regulation of endogenous cardiomyocyte proliferation: The known unknowns.Journal of molecular and cellular cardiology · 2023
    Review
  19. Article
  20. Article

87 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 2 countries.

Sung-Eun KimF. M. Kirby Center, Boston Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.
He Huang
Ming Zhao
Xinjun Zhang
Aili Zhang
Mikhail V Semonov
Bryan T MacDonald
Xiaowu Zhang
Jose Garcia Abreu
Leilei Peng
Xi He
Harvard University · USBoston Children's Hospital · USUniversity of Arizona · USUniversidade Federal do Rio de Janeiro · BR

Funding

SYNAPTIC MECHANISMS IN HIPPOCAMPAL EPILEPTOGENESISP30HD018655 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI POMEROY, SCOTT LOREN · 1985 to 2015
$26.2M
Genetic and Chemical Biological Studies of a Novel Wnt Inhibitor Tiki2R01AR060359 · NIAMS · BOSTON CHILDREN'S HOSPITAL · PI HE, XI · 2011 to 2015
$2.8M
Wnt/beta-catenin signaling: phosphorylation regulation of Wnt receptor-Axin interR01GM074241 · NIGMS · CHILDREN'S HOSPITAL BOSTON · PI HE, XI · 2005 to 2013
$2.5M
High-resolution multi-color FLIM-FRET tomography of whole organismR01EB015481 · NIBIB · UNIVERSITY OF ARIZONA · PI PENG, LEILEI · 2012 to 2015
$1.3M
Densely Multiplexed Fluorescence Imaging by Fourier Transform FluorometryR00EB008737 · NIBIB · UNIVERSITY OF ARIZONA · PI PENG, LEILEI · 2009 to 2011
$731k
CIHRNIAMS NIH HHS R01 AR060359NIBIB NIH HHS R00 EB008737NIBIB NIH HHS R00EB008737NIBIB NIH HHS R01 EB015481NIBIB NIH HHS R01EB015481NICHD NIH HHS P30 HD018655NICHD NIH HHS P30 HD-18655NIGMS NIH HHS R01 GM074241
6 · The paper itself

Abstract

Wnt signaling stabilizes β-catenin through the LRP6 receptor signaling complex, which antagonizes the β-catenin destruction complex. The Axin scaffold and associated glycogen synthase kinase-3 (GSK3) have central roles in both assemblies, but the transduction mechanism from the receptor to the destruction complex is contentious. We report that Wnt signaling is governed by phosphorylation regulation of the Axin scaffolding function. Phosphorylation by GSK3 kept Axin activated ("open") for β-catenin interaction and poised for engagement of LRP6. Formation of the Wnt-induced LRP6-Axin signaling complex promoted Axin dephosphorylation by protein phosphatase-1 and inactivated ("closed") Axin through an intramolecular interaction. Inactivation of Axin diminished its association with β-catenin and LRP6, thereby inhibiting β-catenin phosphorylation and enabling activated LRP6 to selectively recruit active Axin for inactivation reiteratively. Our findings reveal mechanisms for scaffold regulation and morphogen signaling.

Indexed as

Amino Acid SequenceAnimalsAxin Proteinbeta CateninGlycogen Synthase Kinase 3HEK293 CellsHeLa CellsHumansLow Density Lipoprotein Receptor-Related Protein-6Molecular Sequence DataPhosphorylationProtein StabilitySignal TransductionWnt ProteinsXenopusAxin Proteinbeta CateninGlycogen Synthase Kinase 3Low Density Lipoprotein Receptor-Related Protein-6Wnt Proteins

Identifiers

PMID23579495
PMCPMC3788643
OpenAlexW2050126707

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.