Evidence map›Paper›PMID 25468996›Full record

ArticleScience signaling2014

E-cadherin interactome complexity and robustness resolved by quantitative proteomics.

Zhenhuan Guo, Lisa J Neilson, Hang Zhong, Paul S Murray, Sara Zanivan, Ronen Zaidel-Bar

Abstract read
In one paragraph

Article in Science signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed, 1 pooled it
7.0field-weighted citation impact, top 2% 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

116 citing papers in PubMed, 1 synthesis or guideline pooled it, 195 citations in OpenAlex.

  1. Pooled it
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  11. Identification of PKN2 and MOB4 as Coordinators of Collective Cell Migration.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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56 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Zhenhuan GuoMechanobiology Institute of Singapore, National University of Singapore, Singapore 117411, Singapore.
Lisa J NeilsonVascular Proteomics Laboratory, Cancer Research UK Beatson Institute, Glasgow G61 1BD, UK.
Hang ZhongMechanobiology Institute of Singapore, National University of Singapore, Singapore 117411, Singapore.
Paul S MurrayDepartments of Biochemistry and Molecular Biophysics and Systems Biology, and Center of Computational Biology and Bioinformatics, Columbia University, New York, NY 10032, USA.
Sara ZanivanVascular Proteomics Laboratory, Cancer Research UK Beatson Institute, Glasgow G61 1BD, UK.
Ronen Zaidel-BarMechanobiology Institute of Singapore, National University of Singapore, Singapore 117411, Singapore. Department of Biomedical Engineering, National University of Singapore, Singapore 117575, Singapore. biezbr@nus.edu.sg.
National University of Singapore · SG

Funding

Cancer Research UK 12935Cancer Research UK A12935
6 · The paper itself

Abstract

E-cadherin-mediated cell-cell adhesion and signaling plays an essential role in development and maintenance of healthy epithelial tissues. Adhesiveness mediated by E-cadherin is conferred by its extracellular cadherin domains and is regulated by an assembly of intracellular adaptors and enzymes associated with its cytoplasmic tail. We used proximity biotinylation and quantitative proteomics to identify 561 proteins in the vicinity of the cytoplasmic tail of E-cadherin. In addition, we used proteomics to identify proteins associated with E-cadherin-containing adhesion plaques from a cell-glass interface, which enabled the assignment of cellular localization to putative E-cadherin-interacting proteins. Moreover, by tagging identified proteins with GFP (green fluorescent protein), we determined the subcellular localization of 83 putative E-cadherin-proximal proteins and identified 24 proteins that were previously uncharacterized as part of adherens junctions. We constructed and characterized a comprehensive E-cadherin interaction network of 79 published and 394 previously uncharacterized proteins using a structure-informed database of protein-protein interactions. Finally, we found that calcium chelation, which disrupts the interaction of the extracellular E-cadherin domains, did not disrupt most intracellular protein interactions with E-cadherin, suggesting that the E-cadherin intracellular interactome is predominantly independent of cell-cell adhesion.

Indexed as

CadherinsCalcium Chelating AgentsCarbon-Nitrogen LigasesCell AdhesionCell Line, TumorComputational BiologyEpitheliumEscherichia coli ProteinsGreen Fluorescent ProteinsHumansMass SpectrometryMicroscopy, ConfocalProtein Interaction MappingProteomicsRepressor ProteinsbirA protein, E coliCadherinsCalcium Chelating AgentsCarbon-Nitrogen LigasesEscherichia coli ProteinsGreen Fluorescent ProteinsRepressor Proteins

Identifiers

PMID25468996
PMCPMC4972397
OpenAlexW1971253408

What OpenQuestion holds

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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.