Evidence map›Paper›PMID 33229577›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Mapping transmembrane binding partners for E-cadherin ectodomains.

Omer Shafraz, Bin Xie, Soichiro Yamada, Sanjeevi Sivasankar

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. MappingmBio · 2025
    Article
  9. On-Demand Proximity Labeling Using Light-Activated BioID.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Cell-cell communication: new insights and clinical implications.Signal transduction and targeted therapy · 2024
    Review
  11. Article
  12. Proximitomics by Reactive Species.ACS central science · 2024
    Review
  13. Expression of E-cadherin by CD8Nature communications · 2024
    Article
  14. Article
  15. Article
  16. Review
  17. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  18. Article
  19. Review
  20. 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.

Omer ShafrazDepartment of Biomedical Engineering, University of California, Davis, CA 95616.
Bin XieBiophysics Graduate Group, University of California, Davis, CA 95616.ORCID 0000-0002-2305-7865
Soichiro YamadaDepartment of Biomedical Engineering, University of California, Davis, CA 95616.
Sanjeevi SivasankarDepartment of Biomedical Engineering, University of California, Davis, CA 95616; ssivasankar@ucdavis.edu.ORCID 0000-0003-2593-0477
University of California, Davis · US

Funding

Microscope for ultrasensitive measurement of single-molecule interaction and conformationR01GM121885 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SIVASANKAR, SANJEEVI · 2017 to 2024
$2.5M
Identification of stretch-induced biotinylation at cadherin junctionsR03EB021636 · NIBIB · UNIVERSITY OF CALIFORNIA AT DAVIS · PI YAMADA, SOICHIRO · 2016 to 2017
$141k
NIBIB NIH HHS R03 EB021636NIGMS NIH HHS R01 GM121885
6 · The paper itself

Abstract

We combine proximity labeling and single molecule binding assays to discover transmembrane protein interactions in cells. We first screen for candidate binding partners by tagging the extracellular and cytoplasmic regions of a "bait" protein with BioID biotin ligase and identify proximal proteins that are biotin tagged on both their extracellular and intracellular regions. We then test direct binding interactions between proximal proteins and the bait, using single molecule atomic force microscope binding assays. Using this approach, we identify binding partners for the extracellular region of E-cadherin, an essential cell-cell adhesion protein. We show that the desmosomal proteins desmoglein-2 and desmocollin-3, the focal adhesion protein integrin-α2β1, the receptor tyrosine kinase ligand ephrin-B1, and the classical cadherin P-cadherin, all directly interact with E-cadherin ectodomains. Our data shows that combining extracellular and cytoplasmic proximal tagging with a biophysical binding assay increases the precision with which transmembrane ectodomain interactors can be identified.

Indexed as

CadherinsCell AdhesionCytoplasmDesmocollinsDesmoglein 2DesmoplakinsDesmosomesEphrin-B1HumansIntegrinsMicroscopy, Atomic ForceProtein BindingProtein DomainsProtein Interaction MapsSingle Molecule ImagingCadherinsDesmocollinsDesmoglein 2DesmoplakinsEphrin-B1Integrinsatomic force microscopyBioIDcadherinheterophilic bindingproteomics

Identifiers

PMID33229577
PMCPMC7733791
OpenAlexW3106567593

What OpenQuestion holds

Textmetadata
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.