Evidence map›Paper›PMID 26232493›Full record

ArticleThe Biochemical journal2015

Unliganded EphA3 dimerization promoted by the SAM domain.

Deo R Singh, QingQing Cao, Christopher King, Matt Salotto, Fozia Ahmed, Xiang Yang Zhou, Elena B Pasquale, Kalina Hristova

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2015. 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
2.2field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 51 citations in OpenAlex.

  1. Eph receptor signaling complexes in the plasma membrane.Trends in biochemical sciences · 2024
    Review
  2. Article
  3. Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  4. Eph Receptors in Cancer.Biomedicines · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Approaches to Manipulate Ephrin-A:EphA Forward Signaling Pathway.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  17. Revisiting a controversy: The effect of EGF on EGFR dimer stability.Biochimica et biophysica acta. Biomembranes · 2020
    Article
  18. Review
  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

8 authors at 3 institutions in 1 country.

Deo R SinghDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21212, U.S.A.
QingQing CaoDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21212, U.S.A.
Christopher KingProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21212, U.S.A.
Matt SalottoDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21212, U.S.A.
Fozia AhmedDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21212, U.S.A.
Xiang Yang ZhouVaccine Center, The Wistar Institute, Philadelphia, PA 19104, U.S.A.
Elena B PasqualeCancer Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037, U.S.A.
Kalina HristovaDepartment of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21212, U.S.A. Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21212, U.S.A. kh@jhu.edu.
Johns Hopkins University · USDiscovery Institute · USThe Wistar Institute · US

Funding

Targeting Eph receptors in cancerP01CA138390 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI KUHN, PETER · 2010 to 2014
$7.3M
Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
QI-FRET: a new tool in Receptor Tyrosine Kinase researchR01GM095930 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2011 to 2014
$1.4M
NCI NIH HHS CA138390NCI NIH HHS P01 CA138390NIGMS NIH HHS GM068619NIGMS NIH HHS GM095930NIGMS NIH HHS R01 GM068619NIGMS NIH HHS R01 GM095930
6 · The paper itself

Abstract

The erythropoietin-producing hepatocellular carcinoma A3 (EphA3) receptor tyrosine kinase (RTK) regulates morphogenesis during development and is overexpressed and mutated in a variety of cancers. EphA3 activation is believed to follow a 'seeding mechanism' model, in which ligand binding to the monomeric receptor acts as a trigger for signal-productive receptor clustering. We study EphA3 lateral interactions on the surface of live cells and we demonstrate that EphA3 forms dimers in the absence of ligand binding. We further show that these dimers are stabilized by interactions involving the EphA3 sterile α-motif (SAM) domain. The discovery of unliganded EphA3 dimers challenges the current understanding of the chain of EphA3 activation events and suggests that EphA3 may follow the 'pre-formed dimer' model of activation known to be relevant for other receptor tyrosine kinases. The present work also establishes a new role for the SAM domain in promoting Eph receptor lateral interactions and signalling on the cell surface.

Indexed as

Amino Acid MotifsHEK293 CellsHumansProtein MultimerizationProtein Structure, TertiaryReceptor, EphA3Receptor Protein-Tyrosine KinasesSignal TransductionEPHA3 protein, humanReceptor, EphA3Receptor Protein-Tyrosine KinasesdimerizationEphA3SAM domainsignaling

Identifiers

PMID26232493
PMCPMC4692061
OpenAlexW2417598409

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.