Evidence map›Paper›PMID 24966173›Full record

ArticleMolecular biology of the cell2014

E-cadherin phosphorylation occurs during its biosynthesis to promote its cell surface stability and adhesion.

Abbye E McEwen, Meghan T Maher, Rigen Mo, Cara J Gottardi

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.6field-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

41 citing papers in PubMed, 64 citations in OpenAlex.

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  10. WSP fromFrontiers in oncology · 2022
    Article
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  15. Article
  16. The Cross-Talk Between EGFR and E-Cadherin.Frontiers in cell and developmental biology · 2021
    Review
  17. Article
  18. Review
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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

4 authors at 1 institution in 1 country.

Abbye E McEwenDepartment of Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL 60611Driskill Graduate Training Program in Life Sciences, Northwestern University Feinberg School of Medicine, Chicago, IL 60611.
Meghan T MaherDepartment of Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL 60611Driskill Graduate Training Program in Life Sciences, Northwestern University Feinberg School of Medicine, Chicago, IL 60611.
Rigen MoDepartment of Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL 60611Molecular Oncology Group, Kadmon Research Institute, New York, NY 10016.
Cara J GottardiDepartment of Medicine, Northwestern University Feinberg School of Medicine, Chicago, IL 60611 c-gottardi@northwestern.edu.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
Training Program In Lung SciencesT32HL076139 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI KAREN M RIDGE, Jacob I Sznajder · 2004 to 2026
$9.6M
Mechanism of nuclear signaling and cell-cell adhesion by cateninsR01GM076561 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOTTARDI, CARA J · 2006 to 2015
$2.8M
Role for Wnt/beta-catenin signaling in alveolar repair and fibrosisR01HL094643 · NHLBI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOTTARDI, CARA J · 2011 to 2014
$1.5M
The role of E-cadherin phosphorylation in regulating cell-cell adhesionF30CA171944 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MCEWEN, ABBYE ELIZABETH · 2013 to 2014
$83k
NCI NIH HHS CA060553NCI NIH HHS CCSG P30 CA060553NCI NIH HHS F30 CA171944NCI NIH HHS F30 CA171944-01A1NCI NIH HHS P30 CA060553NHLBI NIH HHS HL094643NHLBI NIH HHS R01 HL094643NHLBI NIH HHS T32 HL076139NHLBI NIH HHS T32HL076139NIGMS NIH HHS GM076561NIGMS NIH HHS R01 GM076561
6 · The paper itself

Abstract

E-cadherin is highly phosphorylated within its β-catenin-binding region, and this phosphorylation increases its affinity for β-catenin in vitro. However, the identification of key serines responsible for most cadherin phosphorylation and the adhesive consequences of modification at such serines have remained unknown. In this study, we show that as few as three serines in the β-catenin-binding domain of E-cadherin are responsible for most radioactive phosphate incorporation. These serines are required for binding to β-catenin and the mutual stability of both E-cadherin and β-catenin. Cells expressing a phosphodeficient (3S>A) E-cadherin exhibit minimal cell-cell adhesion due to enhanced endocytosis and degradation through a lysosomal compartment. Conversely, negative charge substitution at these serines (3S>D) antagonizes cadherin endocytosis and restores wild-type levels of adhesion. The cadherin kinase is membrane proximal and modifies the cadherin before it reaches the cell surface. Together these data suggest that E-cadherin phosphorylation is largely constitutive and integral to cadherin-catenin complex formation, surface stability, and function.

Indexed as

Cell AdhesionAnimalsAntigens, CDbeta CateninCadherinsCell LineCell MembraneChlorocebus aethiopsCOS CellsEndocytosisHumansPhosphorylationProtein BindingSerineAntigens, CDbeta CateninCadherinsCDH1 protein, humanCTNNB1 protein, humanSerine

Identifiers

PMID24966173
PMCPMC4142610
OpenAlexW2104982744

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.