Evidence map›Paper›PMID 14535844›Full record

ArticleThe Biochemical journal2004

Tyr-298 in ephrinB1 is critical for an interaction with the Grb4 adaptor protein.

Yong-Sik Bong, Yeon-Hwa Park, Hyun-Shik Lee, Kathleen Mood, Akihiko Ishimura, Ira O Daar

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 30% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Ephrin ligands and Eph receptors contribution to hematopoiesis.Cellular and molecular life sciences : CMLS · 2017
    Review
  7. A frog's view of EphrinB signaling.Genesis (New York, N.Y. : 2000) · 2017
    Review
  8. Review
  9. Article
  10. Article
  11. Non-SH2/PDZ reverse signaling by ephrins.Seminars in cell & developmental biology · 2012
    Review
  12. Article
  13. Eph/ephrin signaling in cell-cell and cell-substrate adhesion.Frontiers in bioscience (Landmark edition) · 2012
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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
  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

6 authors at 1 institution in 1 country.

Yong-Sik BongRegulation of Cell Growth Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, Frederick, MD 21702, USA.
Yeon-Hwa Park
Hyun-Shik Lee
Kathleen Mood
Akihiko Ishimura
Ira O Daar
Frederick National Laboratory for Cancer Research · US

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 and their membrane-bound ligands, the ephrins, are thought to play a role in the regulation of cell adhesion and migration during development by mediating cell-to-cell signalling events. The transmembrane ephrinB protein is a bidirectional signalling molecule that sends a forward signal through the activation of its cognate receptor tyrosine kinase residing on another cell. The reverse signal is transduced into the ephrinB-expressing cell via tyrosine phosphorylation of its conserved C-terminal cytoplasmic domain. Previous work from our laboratory has implicated the activated FGFR1 (fibroblast growth factor receptor 1) as a regulator of a de-adhesion signal that results from overexpression of ephrinB1. In the present study, we report the isolation of Xenopus Grb4 (growth-factor-receptor-bound protein 4), an ephrinB1-interacting protein, and we show that when expressed in Xenopus oocytes, ephrinB1 interacts with Grb4 in the presence of an activated FGFR1. Amino acid substitutions were generated in Grb4, and the resulting mutants were expressed along with ephrinB1 and an activated FGFR in Xenopus oocytes. Co-immunoprecipitation analysis shows that the FLVR motif within the Src homology 2 domain of Xenopus Grb4 is vital for this phosphorylation-dependent interaction with ephrinB1. More importantly, using deletion and substitution analysis we identify the tyrosine residue at position 298 of ephrinB1 as being required for the physical interaction with Grb4, whereas Tyr-305 and Tyr-310 are dispensable. Moreover, we show that the region between amino acids 301 and 304 of ephrinB1 is also required for this critical tyrosine-phosphorylation-dependent event.

Indexed as

Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesCells, CulturedEphrin-B1HumansMolecular Sequence DataOncogene ProteinsPhosphorylationSequence Alignmentsrc Homology DomainsTyrosineXenopus laevisXenopus ProteinsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportEphrin-B1NCK2 protein, humanNCK2 protein, XenopusOncogene ProteinsTyrosineXenopus Proteins

Identifiers

PMID14535844
PMCPMC1223872
OpenAlexW2088323586

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.