Evidence map›Paper›PMID 21606194›Full record

ArticleMolecular and cellular biology2011

Coordinated action of CK1 isoforms in canonical Wnt signaling.

Beatriz Del Valle-Pérez, Oriol Arqués, Meritxell Vinyoles, Antonio García de Herreros, Mireia Duñach

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

53 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
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  8. Isoform-specific C-terminal phosphorylation drives autoinhibition of Casein kinase 1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. The Chronic Toxicity of Endocrine-Disrupting Chemical toInternational journal of molecular sciences · 2024
    Article
  10. Article
  11. The interplay between Wnt signaling pathways and microtubule dynamics.In vitro cellular & developmental biology. Animal · 2024
    Review
  12. Article
  13. Article
  14. Superresolution microscopy localizes endogenous Dvl2 to Wnt signaling-responsive biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Beatriz Del Valle-PérezDepartament de Bioquímica i Biologia Molecular, CEB, Facultat de Medicina, Universitat Autònoma de Barcelona, E-08193 Bellaterra, Spain.
Oriol Arqués
Meritxell Vinyoles
Antonio García de Herreros
Mireia Duñach
Universitat Autònoma de Barcelona · ESHospital Del Mar · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the Wnt pathway promotes the progressive phosphorylation of coreceptor LRP5/6 (low-density lipoprotein receptor-related proteins 5 and 6), creating a phosphorylated motif that inhibits glycogen synthase kinase 3β (GSK-3β), which in turn stabilizes β-catenin, increasing the transcription of β-catenin target genes. Casein kinase 1 (CK1) kinase family members play a complex role in this pathway, either as inhibitors or as activators. In this report, we have dissected the roles of CK1 isoforms in the early steps of Wnt signaling. CK1ε is constitutively bound to LRP5/6 through its interaction with p120-catenin and E-cadherin or N-cadherin and is activated upon Wnt3a stimulation. CK1α also associates with the LRP5/6/p120-catenin complex but, differently from CK1ε, only after Wnt3a addition. Binding of CK1α is dependent on CK1ε and occurs in a complex with axin. The two protein kinases function sequentially: whereas CK1ε is required for early responses to Wnt3a stimulation, such as recruitment of Dishevelled 2 (Dvl-2), CK1α participates in the release of p120-catenin from the complex, which activates p120-catenin for further actions on this pathway. Another CK1, CK1γ, acts at an intermediate level, since it is not necessary for Dvl-2 recruitment but for LRP5/6 phosphorylation at Thr1479 and axin binding. Therefore, our results indicate that CK1 isoforms work coordinately to promote the full response to Wnt stimulus.

Indexed as

Adaptor Proteins, Signal TransducingAxin ProteinCasein Kinase ICateninsCell LineDelta CateninDishevelled ProteinsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHEK293 CellsHumansIsoenzymesLDL-Receptor Related ProteinsLow Density Lipoprotein Receptor-Related Protein-5Low Density Lipoprotein Receptor-Related Protein-6PhosphoproteinsAdaptor Proteins, Signal TransducingAxin ProteinCasein Kinase ICateninsCTNND1 protein, humanDelta CateninDishevelled ProteinsDVL2 protein, humanGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanIsoenzymesLDL-Receptor Related ProteinsLow Density Lipoprotein Receptor-Related Protein-5Low Density Lipoprotein Receptor-Related Protein-6LRP5 protein, humanLRP6 protein, humanPhosphoproteinsRecombinant Fusion ProteinsRepressor ProteinsRNA, Small InterferingWnt3A ProteinWNT3A protein, humanWnt3 ProteinWnt Proteins

Identifiers

PMID21606194
PMCPMC3133391
OpenAlexW2165235649

What OpenQuestion holds

Textmetadata
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.