Evidence map›Paper›PMID 24503895›Full record

ArticlePloS one2014

Trans-homophilic interaction of CADM1 activates PI3K by forming a complex with MAGuK-family proteins MPP3 and Dlg.

Shigefumi Murakami, Mika Sakurai-Yageta, Tomoko Maruyama, Yoshinori Murakami

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  8. Oncology letters · 2022
    Article
  9. Article
  10. Review
  11. Review
  12. The Role of Cell Adhesion Molecule 1 (CADM1) in Cutaneous Malignancies.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Shigefumi MurakamiDivision of Molecular Pathology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Mika Sakurai-YagetaDivision of Molecular Pathology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Tomoko MaruyamaDivision of Molecular Pathology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Yoshinori MurakamiDivision of Molecular Pathology, Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CADM1 (Cell adhesion molecule 1), a cell adhesion molecule belonging to the immunoglobulin superfamily, is involved in cell-cell interaction and the formation and maintenance of epithelial structure. Expression of CADM1 is frequently down-regulated in various tumors derived from epithelial cells. However, the intracellular signaling pathways activated by CADM1-mediated cell adhesion remain unknown. Here, we established a cell-based spreading assay to analyze the signaling pathway specifically activated by the trans-homophilic interaction of CADM1. In the assay, MDCK cells expressing exogenous CADM1 were incubated on the glass coated with a recombinant extracellular fragment of CADM1, and the degree of cell spreading was quantified by measuring their surface area. Assay screening of 104 chemical inhibitors with known functions revealed that LY294002, an inhibitor of phosphoinositide 3-kinase (PI3K), efficiently suppressed cell spreading in a dose-dependent manner. Inhibitors of Akt and Rac1, downstream effectors of PI3K, also partially suppressed cell spreading, while the addition of both inhibitors blocked cell spreading to the same extent as did LY294002. Furthermore, MPP3 and Dlg, membrane-associated guanylate kinase homologs (MAGuK) proteins, connect CADM1 with p85 of PI3K by forming a multi-protein complex at the periphery of cells. These results suggest that trans-homophilic interaction mediated by CADM1 activates the PI3K pathway to reorganize the actin cytoskeleton and form epithelial cell structure.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell Adhesion Molecule-1Cell Adhesion MoleculesCell MovementClass Ia Phosphatidylinositol 3-KinaseDiscs Large Homolog 1 ProteinDogsEnzyme ActivationHEK293 CellsHumansImmunoglobulinsMadin Darby Canine Kidney CellsMembrane ProteinsNuclear ProteinsProtein BindingAdaptor Proteins, Signal TransducingCADM1 protein, humanCell Adhesion Molecule-1Cell Adhesion MoleculesClass Ia Phosphatidylinositol 3-KinaseDiscs Large Homolog 1 ProteinDLG1 protein, humanDLG3 protein, humanImmunoglobulinsMembrane ProteinsNuclear ProteinsProtein Kinase InhibitorsProto-Oncogene Proteins c-aktrac1 GTP-Binding ProteinRecombinant ProteinsTranscription Factors

Identifiers

PMID24503895
PMCPMC3913574
OpenAlexW2060615170

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.