Evidence map›Paper›PMID 17954917›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

ephrinB1 signals from the cell surface to the nucleus by recruitment of STAT3.

Yong-Sik Bong, Hyun-Shik Lee, Laura Carim-Todd, Kathleen Mood, Tagvor G Nishanian, Lino Tessarollo, Ira O Daar

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

55 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. LIM-domain-only 4 (LMO4) enhances CD8Signal transduction and targeted therapy · 2024
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. EphrinB2-EphB4 Signaling in Neurooncological Disease.International journal of molecular sciences · 2022
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Functional Consequences of Synapse Remodeling Following Astrocyte-Specific Regulation of Ephrin-B1 in the Adult Hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  14. Article
  15. From Neural Crest Development to Cancer and Vice Versa: How p75Frontiers in molecular neuroscience · 2018
    Review
  16. Article
  17. Review
  18. Ephrin ligands and Eph receptors contribution to hematopoiesis.Cellular and molecular life sciences : CMLS · 2017
    Review
  19. Article
  20. Eph/ephrin signaling in the kidney and lower urinary tract.Pediatric nephrology (Berlin, Germany) · 2016
    Review
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.

Yong-Sik BongLaboratory of Cell and Developmental Signaling and Mouse Cancer Genetics Program, National Cancer Institute, Frederick, MD 21702, USA.
Hyun-Shik Lee
Laura Carim-Todd
Kathleen Mood
Tagvor G Nishanian
Lino Tessarollo
Ira O Daar
Toxicologie, Pharmacologie et Signalisation Cellulaire · FRNational Cancer Institute · 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
Intramural NIH HHS
6 · The paper itself

Abstract

The Eph (erythropoietin-producing hepatoma) family of receptor tyrosine kinases and their membrane-bound ligands, the ephrins, have been implicated in regulating cell adhesion and migration during development by mediating cell-to-cell signaling events. The transmembrane ephrinB (Eph receptor interactor B) protein is a bidirectional signaling molecule that sends a forward signal through the activation of its cognate receptor tyrosine kinase, residing on another cell. A reverse signal can be transduced into the ephrinB-expressing cell via tyrosine phosphorylation of its conserved C-terminal cytoplasmic domain. Although some insight has been gained regarding how ephrinB may send signals affecting cytoskeletal components, little is known about how ephrinB1 reverse signaling affects transcriptional processes. Here we report that signal transducer and activator of transcription 3 (STAT3) can interact with ephrinB1 in a phosphorylation-dependent manner that leads to enhanced activation of STAT3 transcriptional activity. This activity depends on the tyrosine kinase Jak2, and two tyrosines within the intracellular domain of ephrinB1 are critical for the association with STAT3 and its activation. The recruitment of STAT3 to ephrinB1, and its resulting Jak2-dependent activation and transcription of reporter targets, reveals a signaling pathway from ephrinB1 to the nucleus.

Indexed as

Signal TransductionActive Transport, Cell NucleusAmino Acid SequenceAnimalsCell LineCell MembraneCell NucleusChlorocebus aethiopsDNAEphrin-B1HumansJanus Kinase 2Molecular Sequence DataPhosphorylationPhosphotyrosineProtein BindingDNAEphrin-B1Janus Kinase 2PhosphotyrosineSTAT3 Transcription Factor

Identifiers

PMID17954917
PMCPMC2077252
OpenAlexW2150536836

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.