Evidence map›Paper›PMID 26363067›Full record

ArticleThe Journal of biological chemistry2015

EphA2 Receptor Unliganded Dimers Suppress EphA2 Pro-tumorigenic Signaling.

Deo R Singh, Fozia Ahmed, Christopher King, Nisha Gupta, Matt Salotto, Elena B Pasquale, Kalina Hristova

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 64 citations in OpenAlex.

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  18. Approaches to Manipulate Ephrin-A:EphA Forward Signaling Pathway.Pharmaceuticals (Basel, Switzerland) · 2020
    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

7 authors at 2 institutions in 1 country.

Deo R SinghDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
Fozia AhmedDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
Christopher KingDepartment of Program in Molecular Biophysics, The Johns Hopkins University, Baltimore, Maryland 21218 and.
Nisha GuptaDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
Matt SalottoDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland 21218.
Elena B PasqualeSanford Burnham Prebys Medical Discovery Institute, La Jolla, San Diego, California 92037.
Kalina HristovaDepartment of Materials Science and Engineering, The Johns Hopkins University, Baltimore, Maryland 21218; Department of Program in Molecular Biophysics, The Johns Hopkins University, Baltimore, Maryland 21218 and. Electronic address: kh@jhu.edu.
Johns Hopkins University · USDiscovery Institute · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Targeting Eph receptors in cancerP01CA138390 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI PASQUALE, ELENA B · 2010 to 2014
$7.3M
Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
NCI NIH HHS CA138390NCI NIH HHS P01 CA138390NCI NIH HHS P30 CA030199NIGMS NIH HHS GM068619NIGMS NIH HHS R01 GM068619
6 · The paper itself

Abstract

The EphA2 receptor tyrosine kinase promotes cell migration and cancer malignancy through a ligand- and kinase-independent distinctive mechanism that has been linked to high Ser-897 phosphorylation and low tyrosine phosphorylation. Here, we demonstrate that EphA2 forms dimers in the plasma membrane of HEK293T cells in the absence of ephrin ligand binding, suggesting that the current seeding mechanism model of EphA2 activation is incomplete. We also characterize a dimerization-deficient EphA2 mutant that shows enhanced ability to promote cell migration, concomitant with increased Ser-897 phosphorylation and decreased tyrosine phosphorylation compared with EphA2 wild type. Our data reveal a correlation between unliganded dimerization and tumorigenic signaling and suggest that EphA2 pro-tumorigenic activity is mediated by the EphA2 monomer. Thus, a therapeutic strategy that aims at the stabilization of EphA2 dimers may be beneficial for the treatment of cancers linked to EphA2 overexpression.

Indexed as

Amino Acid SubstitutionCell MovementHEK293 CellsHumansLigandsMutagenesis, Site-DirectedOncogene ProteinsOsmotic PressurePhosphorylationProtein Interaction Domains and MotifsProtein MultimerizationProtein StabilityProtein Structure, QuaternaryReceptor, EphA2Signal TransductionLigandsOncogene ProteinsReceptor, EphA2dimerizationmembrane proteinreceptor tyrosine kinasesignal transductionthermodynamics

Identifiers

PMID26363067
PMCPMC4646390
OpenAlexW2175619235

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.