Evidence map›Paper›PMID 25568338›Full record

ArticleMolecular biology of the cell2015

Distinct functionality of dishevelled isoforms on Ca2+/calmodulin-dependent protein kinase 2 (CamKII) in Xenopus gastrulation.

Marc Gentzel, Carolin Schille, Verena Rauschenberger, Alexandra Schambony

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Decoding Dishevelled-Mediated Wnt Signaling in Vertebrate Early Development.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Dishevelled Paralogs in Vertebrate Development: Redundant or Distinct?Frontiers in cell and developmental biology · 2017
    Review
  14. Review
  15. Article
  16. Article
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

4 authors at 2 institutions in 1 country.

Marc GentzelMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.
Carolin SchilleBiology Department, Developmental Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91058 Erlangen, Germany.
Verena RauschenbergerBiology Department, Developmental Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91058 Erlangen, Germany.
Alexandra SchambonyBiology Department, Developmental Biology, Friedrich-Alexander University Erlangen-Nuremberg, 91058 Erlangen, Germany.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wnt ligands trigger the activation of a variety of β-catenin-dependent and β-catenin-independent intracellular signaling cascades. Despite the variations in intracellular signaling, Wnt pathways share the effector proteins frizzled, dishevelled, and β-arrestin. It is unclear how the specific activation of individual branches and the integration of multiple signals are achieved. We hypothesized that the composition of dishevelled-β-arrestin protein complexes contributes to signal specificity and identified CamKII as an interaction partner of the dishevelled-β-arrestin protein complex by quantitative functional proteomics. Specifically, we found that CamKII isoforms interact differentially with the three vertebrate dishevelled proteins. Dvl1 is required for the activation of CamKII and PKC in the Wnt/Ca(2+) pathway. However, CamKII interacts with Dvl2 but not with Dvl1, and Dvl2 is necessary to mediate CamKII function downstream of Dvl1 in convergent extension movements in Xenopus gastrulation. Our findings indicate that the different Dvl proteins and the composition of dishevelled-β-arrestin protein complexes contribute to the specific activation of individual branches of Wnt signaling.

Indexed as

GastrulationAdaptor Proteins, Signal TransducingAnimalsArrestinsbeta-ArrestinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Dishevelled ProteinsHumansPhosphoproteinsProtein IsoformsWnt Signaling PathwayXenopus laevisXenopus ProteinsAdaptor Proteins, Signal TransducingArrestinsbeta-ArrestinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Dishevelled ProteinsDVL1 protein, humanDVL1 protein, XenopusDVL2 protein, humanPhosphoproteinsProtein IsoformsXenopus Proteins

Identifiers

PMID25568338
PMCPMC4342031
OpenAlexW2097829102

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.