Evidence map›Paper›PMID 22261062›Full record

ArticleBiophysical journal2011

EphA2 receptor activation by monomeric Ephrin-A1 on supported membranes.

Qian Xu, Wan-Chen Lin, Rebecca S Petit, Jay T Groves

Abstract read
In one paragraph

Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Targeting the EphA2 pathway: could it be the way for bone sarcomas?Cell communication and signaling : CCS · 2024
    Review
  2. Article
  3. Article
  4. Geometric Control of Cell Behavior by Biomolecule Nanodistribution.ACS biomaterials science & engineering · 2022
    Article
  5. Article
  6. Article
  7. Phase separation in immune signalling.Nature reviews. Immunology · 2022
    Review
  8. Article
  9. Targeting EphA2 in cancer.Journal of hematology & oncology · 2020
    Review
  10. Approaches to Manipulate Ephrin-A:EphA Forward Signaling Pathway.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  11. Cells · 2020
    Article
  12. Discoidin domain receptors: Micro insights into macro assemblies.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  13. Article
  14. Pinpointed Stimulation of EphA2 Receptors via DNA-Templated Oligovalence.International journal of molecular sciences · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. E-cadherin junction formation involves an active kinetic nucleation process.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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.

Qian XuHoward Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, California, USA.
Wan-Chen Lin
Rebecca S Petit
Jay T Groves

Funding

TRANS-NETWORK PROJECTSU54CA143836 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI LIPHARDT, JAN T. · 2009 to 2014
$15.1M
Howard Hughes Medical InstituteNCI NIH HHS U54 CA143836
6 · The paper itself

Abstract

The receptor tyrosine kinase EphA2 interacts with its glycosylphosphatidylinositol (GPI)-linked ephrin-A1 ligand in a juxtacrine configuration. The soluble ephrin-A1 protein, without its GPI membrane linker, fails to activate EphA2. However, preclustered ephrin-A1 protein is active in solution and has been frequently used to trigger the EphA2 receptor. Although this approach has yielded insights into EphA2 signaling, preclustered ligands bypass natural receptor clustering processes and thus mask any role of clustering as a signal regulatory mechanism. Here, we present EphA2-expressing cells with a fusion protein of monomeric ephrin-A1 (mEA1) and enhanced monomeric yellow fluorescent protein that is linked to a supported lipid bilayer via a nickel-decahistidine anchor. The mEA1 is homogeneously dispersed, laterally mobile, and monomeric as measured by fluorescence imaging, correlation spectroscopy, and photon counting histogram analysis, respectively. Ephrin-A1 presented in this manner activates EphA2 on the surface of MDA-MB-231 human breast cancer cells, as measured by EphA2 phosphorylation and degradation. Spatial mutation experiments in which nanopatterns on the underlying substrate restrict mEA1 movement in the supported lipid bilayer reveal spatio-mechanical regulation of this signaling pathway, consistent with recently reported observations using a synthetically cross-linked ephrin-A1 dimer.

Indexed as

Bacterial ProteinsBlotting, WesternCell ExtractsCell Line, TumorEnzyme ActivationEphrin-A1Fluorescent Antibody TechniqueHumansLipid BilayersLuminescent ProteinsProtein BindingReceptor, EphA2Recombinant Fusion ProteinsSignal TransductionSurface PropertiesBacterial ProteinsCell ExtractsEphrin-A1Lipid BilayersLuminescent ProteinsReceptor, EphA2Recombinant Fusion Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID22261062
PMCPMC3297811

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.