Evidence map›Paper›PMID 28549925›Full record

ArticleJournal of molecular biology2017

Intracellular Domain Contacts Contribute to Ecadherin Constitutive Dimerization in the Plasma Membrane.

Deo R Singh, Fozia Ahmed, Sarvenaz Sarabipour, Kalina Hristova

Abstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Revisiting a controversy: The effect of EGF on EGFR dimer stability.Biochimica et biophysica acta. Biomembranes · 2020
    Article
  19. Article
  20. Cadherin Extracellular Domain Clustering in the Absence ofThe journal of physical chemistry letters · 2019
    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 1 institution in 1 country.

Deo R SinghDepartment of Materials Science and Engineering and Institute of NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, USA.
Fozia AhmedDepartment of Materials Science and Engineering and Institute of NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, USA.
Sarvenaz SarabipourDepartment of Materials Science and Engineering and Institute of NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, USA.
Kalina HristovaDepartment of Materials Science and Engineering and Institute of NanoBioTechnology, Johns Hopkins University, 3400 Charles Street, Baltimore, MD 21218, USA. Electronic address: kh@jhu.edu.
Johns Hopkins University · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

Epithelial cadherin (Ecadherin) is responsible for the intercellular cohesion of epithelial tissues. It forms lateral clusters within adherens cell-cell junctions, but its association state outside these clusters is unknown. Here, we use a quantitative Forster resonance energy transfer (FRET) approach to show that Ecadherin forms constitutive dimers and that these dimers exist independently of the actin cytoskeleton or cytoplasmic proteins. The dimers are stabilized by intermolecular contacts that occur along the entire length of Ecadherin, with the intracellular domains having a surprisingly strong favorable contribution. We further show that Ecadherin mutations and calcium depletion induce structural alterations that propagate from the N terminus all the way to the C terminus, without destabilizing the dimeric state. These findings provide context for the interpretation of Ecadherin adhesion experiments. They also suggest that early events of adherens junction assembly involve interactions between from preformed Ecadherin dimers.

Indexed as

Protein MultimerizationCadherinsCalciumCell LineCell MembraneDNA Mutational AnalysisFluorescence Resonance Energy TransferHumansCadherinsCalciumdimerizationEcadherinmembrane protein

Identifiers

PMID28549925
PMCPMC5528180
OpenAlexW2618701107

What OpenQuestion holds

Textmetadata
LicenceTDM
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.