Evidence map›Paper›PMID 14742708›Full record

ArticleMolecular biology of the cell2004

Ectopic EphA4 receptor induces posterior protrusions via FGF signaling in Xenopus embryos.

Eui Kyun Park, Neil Warner, Yong-Sik Bong, David Stapleton, Ryu Maeda, Tony Pawson, Ira O Daar

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. A Novel Occulta-Type Spina Bifida Mediated by Murine Double HeterozygotesFrontiers in cell and developmental biology · 2017
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Eph-dependent cell-cell adhesion and segregation in development and cancer.Cellular and molecular life sciences : CMLS · 2012
    Review
  9. Review
  10. EphA receptor signaling--complexity and emerging themes.Seminars in cell & developmental biology · 2012
    Review
  11. Article
  12. Article
  13. Eph/ephrin signaling in cell-cell and cell-substrate adhesion.Frontiers in bioscience (Landmark edition) · 2012
    Review
  14. Article
  15. Eph/ephrin signaling: networks.Genes & development · 2008
    Review
  16. ephrinB1 signals from the cell surface to the nucleus by recruitment of STAT3.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  17. Article
  18. Article
  19. 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

7 authors at 2 institutions in 2 countries.

Eui Kyun ParkRegulation of Cell Growth Laboratory, National Cancer Institute-Frederick, Frederick, Maryland 21702, USA.
Neil Warner
Yong-Sik Bong
David Stapleton
Ryu Maeda
Tony Pawson
Ira O Daar
Frederick National Laboratory for Cancer Research · USMount Sinai Hospital · CA

Funding

Mechanisms of Cross-talk Between EphrinB and Alternate Signaling PathwaysZIABC010006 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAAR, IRA · 2009 to 2025
$11.5M
Mechanisms of Cross-talk Between EphrinB and Alternate Signaling PathwaysZ01BC010006 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAAR, IRA OWEN · 1996 to 2008
$1.8M
6 · The paper itself

Abstract

The Eph family of receptor tyrosine kinases regulates numerous biological processes. To examine the biochemical and developmental contributions of specific structural motifs within Eph receptors, wild-type or mutant forms of the EphA4 receptor were ectopically expressed in developing Xenopus embryos. Wild-type EphA4 and a mutant lacking both the SAM domain and PDZ binding motif were constitutively tyrosine phosphorylated in vivo and catalytically active in vitro. EphA4 induced loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures in Xenopus embryos. Moreover, mutation of a conserved SAM domain tyrosine to phenylalanine (Y928F) enhanced the ability of EphA4 to induce these phenotypes, suggesting that the SAM domain may negatively regulate some aspects of EphA4 activity in Xenopus. Analysis of double mutants revealed that the Y928F EphA4 phenotypes were dependent on kinase activity; juxtamembrane sites of tyrosine phosphorylation and SH2 domain-binding were required for cell dissociation, but not for posterior protrusions. The induction of protrusions and expansion of posterior structures is similar to phenotypic effects observed in Xenopus embryos expressing activated FGFR1. Furthermore, the budding ectopic protrusions induced by EphA4 express FGF-8, FGFR1, and FGFR4a. In addition, antisense morpholino oligonucleotide-mediated loss of FGF-8 expression in vivo substantially reduced the phenotypic effects in EphA4Y928F expressing embryos, suggesting a connection between Eph and FGF signaling.

Indexed as

Gene Expression Regulation, DevelopmentalAmino Acid MotifsAnimalsBlotting, WesternCatalysisCell AdhesionCell MembraneCloning, MolecularFibroblast Growth Factor 8Fibroblast Growth FactorsIn Situ HybridizationMiceMutationPhenotypePhosphorylationPrecipitin TestsFibroblast Growth Factor 8Fibroblast Growth FactorsReceptor, EphA4RNARNA, MessengerTyrosine

Identifiers

PMID14742708
PMCPMC379263
OpenAlexW2114355118

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.