Evidence map›Paper›PMID 9233798›Full record

ArticleThe EMBO journal1997

Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells.

S J Holland, N W Gale, G D Gish, R A Roth, Z Songyang, L C Cantley, M Henkemeyer, G D Yancopoulos, T Pawson

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
8.2field-weighted citation impact, top 1% 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

98 citing papers in PubMed, 271 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. NCK1 Modulates Neuronal Actin Dynamics and Promotes Dendritic Spine, Synapse, and Memory Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

38 more citing papers are in PubMed but not listed here.

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

9 authors at 5 institutions in 2 countries.

S J HollandProgramme in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.
N W Gale
G D Gish
R A Roth
Z Songyang
L C Cantley
M Henkemeyer
G D Yancopoulos
T Pawson
Beth Israel Deaconess Hospital · USLunenfeld-Tanenbaum Research Institute · CARegeneron (United States) · USMount Sinai Hospital · CASamueli Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eph-related receptor tyrosine kinases have been implicated in the control of axonal navigation and fasciculation. To investigate the biochemical mechanisms underlying such functions, we have expressed the EphB2 receptor (formerly Nuk/Cek5/Sek3) in neuronal NG108-15 cells, and have observed the tyrosine phosphorylation of multiple cellular proteins upon activation of EphB2 by its ligand, ephrin-B1 (formerly Elk-L/Lerk2). The activated EphB2 receptor induced the tyrosine phosphorylation of a 62-64 kDa protein (p62[dok]), which in turn formed a complex with the Ras GTPase-activating protein (RasGAP) and SH2/SH3 domain adaptor protein Nck. RasGAP also bound through its SH2 domains to tyrosine-phosphorylated EphB2 in vitro, and complexed with activated EphB2 in vivo. We have localized an in vitro RasGAP-binding site to conserved tyrosine residues Y604 and Y610 in the juxtamembrane region of EphB2, and demonstrated that substitution of these amino acids abolishes ephrin-B1-induced signalling events in EphB2-expressing NG108-15 cells. These tyrosine residues are followed by proline at the + 3 position, consistent with the binding specificity of RasGAP SH2 domains determined using a degenerate phosphopeptide library. These results identify an EphB2-activated signalling cascade involving proteins that potentially play a role in axonal guidance and control of cytoskeletal architecture.

Indexed as

DNA-Binding ProteinsRNA-Binding Proteinssrc Homology DomainsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCell LineCell MembraneCOS CellsEphrin-B1GTPase-Activating ProteinsHumansMembrane ProteinsMiceMolecular Sequence DataNeuronsAdaptor Proteins, Signal TransducingDNA-Binding ProteinsDOK1 protein, humanDok1 protein, mouseEphrin-B1GAP-associated protein p62GTPase-Activating ProteinsMembrane ProteinsNck proteinOncogene ProteinsPhenylalaninePhosphoproteinsProteinsras GTPase-Activating ProteinsReceptor, EphB2Receptor Protein-Tyrosine KinasesRecombinant Fusion ProteinsRNA-Binding ProteinsTyrosine

Identifiers

PMID9233798
PMCPMC1170012
OpenAlexW2082494746

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.